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Database: UniProt
Entry: D5EKD8_CORAD
LinkDB: D5EKD8_CORAD
Original site: D5EKD8_CORAD 
ID   D5EKD8_CORAD            Unreviewed;      1551 AA.
AC   D5EKD8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ADE54887.1};
DE            EC=1.4.7.1 {ECO:0000313|EMBL:ADE54887.1};
GN   OrderedLocusNames=Caka_1869 {ECO:0000313|EMBL:ADE54887.1};
OS   Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS   KCTC 12865 / 04OKA010-24).
OC   Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC   Coraliomargaritaceae; Coraliomargarita.
OX   NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE54887.1, ECO:0000313|Proteomes:UP000000925};
RN   [1] {ECO:0000313|EMBL:ADE54887.1, ECO:0000313|Proteomes:UP000000925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC   {ECO:0000313|Proteomes:UP000000925};
RX   PubMed=21304713; DOI=10.4056/sigs.952166;
RA   Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA   Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA   Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Coraliomargarita akajimensis type strain
RT   (04OKA010-24).";
RL   Stand. Genomic Sci. 2:290-299(2010).
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|ARBA:ARBA00001927};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716}.
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DR   EMBL; CP001998; ADE54887.1; -; Genomic_DNA.
DR   RefSeq; WP_013043609.1; NC_014008.1.
DR   STRING; 583355.Caka_1869; -.
DR   MEROPS; C44.003; -.
DR   KEGG; caa:Caka_1869; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_0; -.
DR   OMA; TVFRLQH; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000000925; Chromosome.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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; 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   InterPro; IPR013785; Aldolase_TIM.
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; IPR002932; Glu_synthdom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 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   SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADE54887.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000925}.
FT   DOMAIN          23..424
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          933..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..953
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1551 AA;  169947 MW;  A4E82D14FBB529C8 CRC64;
     MEHTYTQPKA QGLYDPQNEH ENCGIGLIVD MKGRKSHDIV QGALEICVNL DHRGGCGCDP
     ITGDGAGIFI QLPHNFFKAV CKEEAGFDVP EDGDYGVGFV FLSQDQEERT NEENIIGEII
     AEEGFELLGW RDVPVKSEIL GKASKACEPV MRQFFIARGD VCERGLAFER KLYLIRRTAT
     HRIRYSGQDE ESLFYISSLS SRTMTYKGML TTEQLGDYFP DLAHEAMDSA LALTHSRFST
     NTFPSWPRAQ PFRYLCHNGE INTVRGNENW LHARQMQLAS EVFGDDLQKL LPIIREDGSD
     SQKFDNCLEF LVLSGRSLAH AMMMMIPEPW ERHKSMPQFK RDFYEFHACM MEPWDGPASM
     AMSDGVQVGA TLDRNGLRPS RYYVTADDRV ILASEVGVLE GIEPKNVVKK GRLEPGRMFL
     IDMEEGRIVD DAELKEQIAA ENPYGEWLKD NLVPADTLPA PEADQTPADN FETLETRQKA
     FGYTFEDMRF IVGPSAQTGK QPLGSMGNDA PLAVLSDQPQ LMYNYFKQLF AQVTNPPIDP
     IREELVTASV TFIGSEGDLT RPGPESCRMI KFETPLLSDA ELAQLRYINK DGFKATKLPI
     TFEAEVGGMA TGHNSVPEPS ISGKGLEGAL EKLFENADAA IRDGVNILIL SDRKVGPNKA
     PIPALLAVAG LHHHLVRQGT RTRVSIVLES GEPREVQHFA LLLGYGANAI NPYLALETVR
     HLVDRGDLDV DPDKACANFL KANLGGVIKT MSKMGISTVA SYRGAQIFEA IGLNQAVIDK
     YFTKTASRVE GIGLGTIAKE TESRHQKAFA PRDDERDAAL DTGGIYQWRA NGERHLFNPV
     TIHKLQMATR FGDYAVFKEY SDAINDQSKE MFTLRGLMDF KIDESKSIPI EEVEPIEEIM
     KRFKTGAMSY GSISKEAHEA IAIAMNRIGG KSNTGEGGED IDRFTPDENG DSRRSAIKQV
     ASGRFGVTSY YLVNSDEIQI KIVQGAKPGE GGELPGHKVL PQIAKTRGTT PGVGLISPPP
     HHDIYSIEDL AELIHDLKNS NVNARVNVKL VSEVGVGTIA AGVAKAKADV ILVSGYDGGT
     GASPRSSIQH AGAPWELGLA ETNQTLLLND LRSRVVVETD GQLKTGRDVA IACLLGAEEF
     GFATTALVTL GCLMMRVCHK NTCPVGVATQ NPELRKKFNG DAESVVNFMK YIATEVREYM
     AKLGYRSINE MVGQVQNLEM RKAVDHWKAK GLDYSKILYK PEVGPEVGTF CQMKQDHLLD
     KCLDMREILE QAQPAVKDGK AVEINLPIIN TDRVVGTITG AEISRNHGPD GLPEDTVQIN
     LTGSAGQSLG AFCPQGMTFT VTGDTNDYLG KGLSGGKIVV RPSEDSPFVA HENIITGNVC
     FYGATKGEAY IAGMAGERFC VRNSGVEAVI EGVGDHALEY MTGGMVINLG TTGRNLGAGM
     SGGVAYVFDE AGDFVQHSLN PDMVNVYQLI ECGDDEINLV KAKIEKHVEL TGSKRGQAIL
     ADWPAIAGKF LKIMPQDYER VLQAQARAEE RGLKGDDAIL AAFEENVKAG H
//
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