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Database: UniProt
Entry: Q9W374_DROME
LinkDB: Q9W374_DROME
Original site: Q9W374_DROME 
ID   Q9W374_DROME            Unreviewed;      1031 AA.
AC   Q9W374;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 2.
DT   24-JAN-2024, entry version 198.
DE   RecName: Full=Dihydropyrimidine dehydrogenase [NADP(+)] {ECO:0000256|RuleBase:RU364041};
DE            Short=DHPDHase {ECO:0000256|RuleBase:RU364041};
DE            Short=DPD {ECO:0000256|RuleBase:RU364041};
DE            EC=1.3.1.2 {ECO:0000256|RuleBase:RU364041};
DE   AltName: Full=Dihydrothymine dehydrogenase {ECO:0000256|RuleBase:RU364041};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|RuleBase:RU364041};
GN   Name=su(r) {ECO:0000313|EMBL:AAN09247.1,
GN   ECO:0000313|FlyBase:FBgn0086450};
GN   Synonyms=CG2194-RC {ECO:0000313|EMBL:ACD81696.1}, Dmel\CG2194
GN   {ECO:0000313|EMBL:AAN09247.1}, Dreg-3 {ECO:0000313|EMBL:AAN09247.1},
GN   Pyd1 {ECO:0000313|EMBL:AAN09247.1}, pyd1
GN   {ECO:0000313|EMBL:AAN09247.1}, Reg-3 {ECO:0000313|EMBL:AAN09247.1},
GN   Su(r) {ECO:0000313|EMBL:AAN09247.1};
GN   ORFNames=CG2194 {ECO:0000313|EMBL:AAN09247.1,
GN   ECO:0000313|FlyBase:FBgn0086450}, Dmel_CG2194
GN   {ECO:0000313|EMBL:AAN09247.1};
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:AAN09247.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAN09247.1, 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|EMBL:AAN09247.1, 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|EMBL:AAN09247.1, 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|EMBL:AAN09247.1, 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:AAN09247.1, 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:AAN64918.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gojkovic Z., Sandrini M.P.B., Piskur J.;
RT   "Dihydropyrimidine dehydrogenases and the evolution of the pyrimidine
RT   degradation pathway.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:AAN09247.1, 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   [8] {ECO:0000313|EMBL:AAN09247.1}
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   [9] {ECO:0000313|EMBL:AAN09247.1, 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   [10] {ECO:0000313|EMBL:AAN09247.1, 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   [11] {ECO:0000313|EMBL:ACD81696.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:ACD81696.1};
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:AAN09247.1}
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   [13] {ECO:0000313|EMBL:AAN09247.1}
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   [14] {ECO:0000313|EMBL:AAN09247.1}
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   [15] {ECO:0000313|EMBL:AAN09247.1}
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 (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [16] {ECO:0000313|EMBL:AAN09247.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes the
CC       reduction of uracil and thymine. {ECO:0000256|RuleBase:RU364041}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouracil + NADP(+) = H(+) + NADPH + uracil;
CC         Xref=Rhea:RHEA:18093, ChEBI:CHEBI:15378, ChEBI:CHEBI:15901,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU364041};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU364041};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|RuleBase:RU364041};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU364041};
CC       Note=Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms
CC       per subunit. {ECO:0000256|RuleBase:RU364041};
CC   -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004668, ECO:0000256|RuleBase:RU364041}.
CC   -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010804, ECO:0000256|RuleBase:RU364041}.
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DR   EMBL; AE014298; AAN09247.1; -; Genomic_DNA.
DR   EMBL; AF545061; AAN64918.1; -; mRNA.
DR   EMBL; BT032682; ACD81696.1; -; mRNA.
DR   RefSeq; NP_727320.1; NM_167182.2.
DR   AlphaFoldDB; Q9W374; -.
DR   SMR; Q9W374; -.
DR   IntAct; Q9W374; 3.
DR   STRING; 7227.FBpp0071273; -.
DR   PaxDb; 7227-FBpp0071272; -.
DR   DNASU; 31858; -.
DR   EnsemblMetazoa; FBtr0071338; FBpp0071273; FBgn0086450.
DR   GeneID; 31858; -.
DR   KEGG; dme:Dmel_CG2194; -.
DR   UCSC; CG2194-RB; d. melanogaster.
DR   AGR; FB:FBgn0086450; -.
DR   CTD; 31858; -.
DR   FlyBase; FBgn0086450; su(r).
DR   VEuPathDB; VectorBase:FBgn0086450; -.
DR   eggNOG; KOG1799; Eukaryota.
DR   GeneTree; ENSGT00500000044896; -.
DR   HOGENOM; CLU_003991_0_0_1; -.
DR   InParanoid; Q9W374; -.
DR   OMA; AWSIHCQ; -.
DR   OrthoDB; 1211169at2759; -.
DR   Reactome; R-DME-73621; Pyrimidine catabolism.
DR   UniPathway; UPA00070; -.
DR   UniPathway; UPA00131; -.
DR   BioGRID-ORCS; 31858; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 31858; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0086450; Expressed in adult Malpighian tubule (Drosophila) and 19 other cell types or tissues.
DR   ExpressionAtlas; Q9W374; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; ISS:FlyBase.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR   GO; GO:0002058; F:uracil binding; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IGI:FlyBase.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR   GO; GO:0006212; P:uracil catabolic process; IBA:GO_Central.
DR   CDD; cd02940; DHPD_FMN; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   InterPro; IPR005720; Dihydroorotate_DH_dom.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   NCBIfam; TIGR01037; pyrD_sub1_fam; 1.
DR   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF01180; DHO_dh; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF14697; Fer4_21; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S {ECO:0000256|RuleBase:RU364041};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU364041};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364041};
KW   FMN {ECO:0000256|RuleBase:RU364041}; Iron {ECO:0000256|RuleBase:RU364041};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU364041};
KW   Metal-binding {ECO:0000256|RuleBase:RU364041};
KW   NADP {ECO:0000256|RuleBase:RU364041};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364041};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9W374};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803}.
FT   DOMAIN          944..976
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          978..1007
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1031 AA;  111226 MW;  FD3CF291078E19B8 CRC64;
     MSPPQLLSKD SPDIEDLLSL NPRVKTQCSV VPTKQTKENK KHWKRNADHA APPCTTLAND
     FSDIKHTTLS ERGALEEAAR CLKCADAPCQ KSCPTQLDIK SFITSIANKN FYGAAKAIFS
     DNPLGLTCGM VCPTSDLCVG GCNLQASEAG PINIGGLQQF ATEVFKKMGV RQRRTPQAEA
     NPLSQKIALV GGGPASLSCA TFLARLGYRD VTIYERRSYL GGLSAAEIPQ YRLPIDAVNF
     EIDLVRDLGV RIETGRSLGT KDLTIQGLLS TGHDAVFVGI GLPEPKLNPI FAGLQPSNGF
     YTSKNFLPLV SDGSKPGLCA CKAAAGLPKL HGNVIVLGAG DTAFDCATSA LRCGARRVFV
     VFRKGSSGIR AVPEEVELAR DERCELLPYL SPRKVIVKDG LITAMEFCRT EQNENDEWVE
     DEEQTQRLKA NFVISAFGSG LEDQDVKAAL APLQFRGELP VVDRVTMQSS VKQVFLGGDL
     AGVANTTVES VNDGKVAAWS IHCQLQGLPL DTPAALPLFY TDIDAVDISV EMCGIRFENP
     FGLASAPPTT STAMIRRAFE QGWGFVVTKT FGLDKDLVTN VSPRIVRGTT SGYKYGPQQG
     CFLNIELISE KRAEYWLKSI GELKRDFPEK IVIASIMCSF NEEDWTELAI KAEQSGADAL
     ELNLSCPHGM GERGMGLACG QDPELVEQIS RWVRKAVKLP FFIKLTPNIT DIVSIAAAAK
     RGGADGGSAI NTVQGLMGLK ADSTAWPAIG KEQRTTYGGV SGNATRPMAL KAISDIANRV
     PGFPILGIGG IDSGEVALQF IHAGATVLQI CSSVQNQDFT VIEDYCTALK ALLYLKANPP
     PVDGPFWDGQ SPPTPVHQKG KPVVRLTGEG KATLGFFGPY QRQRDIKMAE LRSQKGALWD
     AEQVKATPPA SNGAPNPAPR IKDVIGAALD KIGSYNKLDN KQQKVALIDD DMCINCGKCY
     MTCADSGYQA IEFDKDTHIP HVNDDCTGCT LCVSVCPIID CITMVPKKIP HVIKRGVEEK
     IFYTHALSQC Q
//
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