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Database: UniProt
Entry: M9NFH8_DROME
LinkDB: M9NFH8_DROME
Original site: M9NFH8_DROME 
ID   M9NFH8_DROME            Unreviewed;      2115 AA.
AC   M9NFH8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE            EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN   Name=GS {ECO:0000313|EMBL:AFH04475.1};
GN   Synonyms=Dmel\CG9674 {ECO:0000313|EMBL:AFH04475.1};
GN   ORFNames=CG9674 {ECO:0000313|EMBL:AFH04475.1,
GN   ECO:0000313|FlyBase:FBgn0036663}, Dmel_CG9674
GN   {ECO:0000313|EMBL:AFH04475.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA   An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AFH04475.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [9] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [10] {ECO:0000313|EMBL:AFH04475.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109357; DOI=.1534/g3.115.018929;
RG   FlyBase Consortium;
RA   Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA   Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA   Gelbart W.M., null;
RT   "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT   Throughput Data.";
RL   G3 (Bethesda) 5:1721-1736(2015).
RN   [11] {ECO:0000313|EMBL:AFH04475.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109356; DOI=.1534/g3.115.018937;
RG   FlyBase Consortium;
RA   Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA   Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA   null;
RT   "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL   G3 (Bethesda) 5:1737-1749(2015).
RN   [12] {ECO:0000313|EMBL:AFH04475.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25589440;
RA   Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA   Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA   Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA   de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA   Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA   Karpen G.H., Celniker S.E.;
RT   "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL   Genome Res. 25:445-458(2015).
RN   [13] {ECO:0000313|EMBL:AFH04475.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA   Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN   [14] {ECO:0000313|EMBL:AFH04475.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC         NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58359; EC=1.4.1.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00024267};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000187-2};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|PIRSR:PIRSR000187-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+)
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004944}.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC       {ECO:0000256|ARBA:ARBA00004802}.
CC   -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716}.
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DR   EMBL; AE014296; AFH04475.1; -; Genomic_DNA.
DR   EMBL; AE014296; AGB94666.1; -; Genomic_DNA.
DR   RefSeq; NP_001246804.1; NM_001259875.2.
DR   RefSeq; NP_001261973.1; NM_001275044.1.
DR   AlphaFoldDB; M9NFH8; -.
DR   SMR; M9NFH8; -.
DR   STRING; 7227.FBpp0297083; -.
DR   PaxDb; 7227-FBpp0297083; -.
DR   DNASU; 39878; -.
DR   EnsemblMetazoa; FBtr0305916; FBpp0297083; FBgn0036663.
DR   EnsemblMetazoa; FBtr0333608; FBpp0305785; FBgn0036663.
DR   GeneID; 39878; -.
DR   AGR; FB:FBgn0036663; -.
DR   FlyBase; FBgn0036663; CG9674.
DR   VEuPathDB; VectorBase:FBgn0036663; -.
DR   eggNOG; KOG0399; Eukaryota.
DR   GeneTree; ENSGT00940000172171; -.
DR   InParanoid; M9NFH8; -.
DR   OMA; TVFRLQH; -.
DR   OrthoDB; 20503at2759; -.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00690.
DR   BioGRID-ORCS; 39878; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; Galphas; fly.
DR   GenomeRNAi; 39878; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0036663; Expressed in head capsule and 29 other cell types or tissues.
DR   ExpressionAtlas; M9NFH8; baseline and differential.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016040; F:glutamate synthase (NADH) activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00982; gltB_C; 1.
DR   CDD; cd00713; GltS; 1.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR002489; Glu_synth_asu_C.
DR   InterPro; IPR036485; Glu_synth_asu_C_sf.
DR   InterPro; IPR006982; Glu_synth_centr_N.
DR   InterPro; IPR012220; Glu_synth_euk.
DR   InterPro; IPR002932; Glu_synthdom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF00310; GATase_2; 1.
DR   Pfam; PF04898; Glu_syn_central; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   Pfam; PF01493; GXGXG; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000187; GOGAT; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|PIRSR:PIRSR000187-2};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000187-
KW   2}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AFH04475.1};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M9NFH8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803}.
FT   DOMAIN          88..481
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          26..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        88
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT   BINDING         1203
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT   BINDING         1209
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT   BINDING         1214
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ   SEQUENCE   2115 AA;  232205 MW;  AE4C0C94C74B091C CRC64;
     MAPTITDNCE FECATVEATT TSAITIGDSD NFDSSAIGGS GDNFEESNEL HLNGQQDQDV
     QEEQQQQMPW EAPGKQGLYD PQNEHEACGV GFIVAIDGKR SHKILRDAQT LSERMNHRGA
     CACDNDTGDG AGVLASIPHG LYSKALAKQG VTLPELGDYA TGIFYLDEAQ HAAAEKEFDD
     LAKSLGLEVI AWRTVPSNQS AIGVVARKSE PLSRQVFVRR PAGSDEKAFE RQVFVLRKRA
     SHELIKPGRR FYICSLSDRT VVYKGLFTSD QLWDYYTDLK DPEFETYLAL VHTRFSTNTF
     PSWERAHPLR VLAHNGEINT LRGNVNLMKA REGVMQSDLF GDQLKKLYPV VEPNLSDSGS
     FDCVLEFLTM ASDRSLPESV MTMVPEAWQN DKTMPQEKRD FYQWAACVME PWDGPALISF
     TDGRYIGAVL DRNGLRPSRF YVTKENVLVM ASEVGVYDVD PSQVTLKSRL KPGRMLLVDT
     KEKKLIQDIE LKAKIAKSRP HSEWLQQKMI TLDEIRNANV LNTPPVDELA KLPASERGIF
     DPRLSLFGYS TETVNMLLIP MFKNKKEALG SMGNDAPLAC LSNFQPIPYE YFKQLFAQVT
     NPPIDPFREK VVMSMQCPLG PEANLLQPSA QQVHRIWLTN PILSIPDTQL LKRNTHRGWR
     TKVLDITFQY NEGVQGYIDA IDRICREGYA AAQAGYQLLV ISDRGAGIDG KVAVSALLAL
     GALHHHLIET LQRMKVGIVV ETAEAREVHH ICVLLGYGAD AICPYLAFEL AQALRDDGVI
     APEVNDKQIY AAYAQAIDTG IAKVMAKMGI STLQSYKSAQ IFEAVGLGSD LVAKCFRGTQ
     SRIGGVTLEI LAKEGLQRYQ LTYGKATPDT RILRNPGQYH WRHGGEAHIN EPSSIGSLQE
     AAVNKNLDAF EAFKKTTLDS VKKCALRGQL EFVTDRQSID ISEVEPASEI VKRFATGAMS
     FGSISLEAHQ TLSITMNRIG GKSNTGEGGE DSDRYLNQDP NNSRRSAIKQ VASGRFGVTA
     SYLANADDLQ IKMAQGAKPG EGGELPGYKV TKDIAKTRKS VPGVGLISPP PHHDIYSIED
     LAELIYDLKC SNPNARISVK LVSEVGVGVV ASGVAKGKAE HIVISGHDGG TGASSWTGIK
     NAGLPWELGV AETHQVLVLN NLRSRVIVQA DGQLRTGFDV VVAALLGADE FGFSTAPLIV
     MGCTMMRKCH LNTCPVGIAT QDPELRKKFT GKPEHVINFF FMLAEDIRKI MAGLGIRKFQ
     DLIGRTDLLR VASQRDAKAS NLDLKLLLQP ALELRPGTNI VGGSVKQDFQ LEKRSDNELI
     AKAQQIFSGA DDNVTVKMRI HNEERAFGST LSYHIACKYG EAGLPAGKSI DIFLEGSAGQ
     SFCAFLARGV NVTLKGDAND YVGKGLCGGN VVIMPQDTVP FESHLNVIVG NVCLYGATEG
     TAYFRGIASE RFCVRNSGVT AVVEGVGDHG CEYMTGGVVV ILGLTGRNFA AGMSGGIAYV
     YDLDGSFKPK VNPESVELLP LEIEKDVLLV KELLADFIEK TGSKVAKELL DNWAEAQGKF
     VKVFPYEYQK ALKDMAEQQA VEQPLKSAIE NGNGKHEPHI KDIEEAIQDV VLEQKRADRV
     LDKTRGFVKY KRESAPYRDA GERQKDWDEV YNFPHVRKNL KVQAARCMEC GVPFCQSNST
     GCPLGNIIPK WNDLVFHGEW QEALRQLLQT NNFPEFTGRV CPAPCEGSCV LGISEPAVTI
     KNIECAIIDH AFEQGWIKPE IPEVRTGKRV AIVGSGPSGL AASQQLNRAG HFVTVFERND
     RVGGLLQYGI PTMKLSKEVV KRRVDLMADE GIEFRTNVHV GKDLKAEQLL QEYDAVLLTT
     GSTWPRDLPL ANRDLKGIHF AMEFLEAQQK KQLGGKNDII SAAGKNVIII GGGDTGCDCI
     ATSLRQGAKS ITTFEILPEP PQKRAQDNPW PQWPKVFRVD YGHEEVKLKW GKDPRQYCTT
     TKEFVGENGA IKGVNTVEVE WTKTETGQWR MQEVAGSEKY FPADLILLAM GFLGPEKTVP
     SELGLELDPR GNIKASNGQY GTSNSKVFAA GDCRRGQSLV VWAITEGRQA ARQVDSYLTG
     RPSGLPGPGG VIATS
//
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