GLTB_SYNY3
ID GLTB_SYNY3 Reviewed; 1550 AA.
AC P55037;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ferredoxin-dependent glutamate synthase 1;
DE EC=1.4.7.1;
DE AltName: Full=Fd-GOGAT;
GN Name=gltB; OrderedLocusNames=sll1502;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7727752; DOI=10.1007/bf00020228;
RA Navarro F., Chavez S., Candau P., Florencio F.J.;
RT "Existence of two ferredoxin-glutamate synthases in the cyanobacterium
RT Synechocystis sp. PCC 6803. Isolation and insertional inactivation of gltB
RT and gltS genes.";
RL Plant Mol. Biol. 27:753-767(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-
CC oxoglutarate + 2 H(+) + L-glutamine + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:12128, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58359; EC=1.4.7.1;
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Note=Binds 1 [3Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin
CC route): step 1/1.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC -!- INTERACTION:
CC P55037; P52231: trxA; NbExp=2; IntAct=EBI-862093, EBI-862916;
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X80485; CAA56652.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17018.1; -; Genomic_DNA.
DR PIR; S60228; S60228.
DR AlphaFoldDB; P55037; -.
DR SMR; P55037; -.
DR IntAct; P55037; 3.
DR STRING; 1148.1652093; -.
DR MEROPS; C44.003; -.
DR PaxDb; P55037; -.
DR PRIDE; P55037; -.
DR EnsemblBacteria; BAA17018; BAA17018; BAA17018.
DR KEGG; syn:sll1502; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR InParanoid; P55037; -.
DR OMA; TVFRLQH; -.
DR PhylomeDB; P55037; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00691.
DR Proteomes; UP000001425; 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:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; cd02808; GltS_FMN; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.60.20.10; -; 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 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; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Amino-acid biosynthesis; FAD; Flavoprotein; FMN;
KW Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..1550
FT /note="Ferredoxin-dependent glutamate synthase 1"
FT /id="PRO_0000170793"
FT DOMAIN 43..440
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 925..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1097..1154
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1150
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1156
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1161
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1550 AA; 169071 MW; 07AA64D832296943 CRC64;
MPCHEGLHPL VPNFCTVTSP MNSSHLAPQV QGLYDPQNEH DACGVGFIVQ MKGKVSHDIV
EQGLQMLVNL EHRGACGCEP NTGDGAGILI QVPHKFIQKI AGAEGITIPA PGQYAVGNIY
GSPDPLARAE ARQKFNDIVA QEGLKVLGWR DIPTQNEPLG ETAIASEPFM QQVYIARPEG
LTDDLDFERK LYVIRKLTHG AIRSPKIDTY WYVASLSART LVYKGMLTTA QVGQYYPELH
DPDMESALAL VHSRFSTNTF PSWERSHPYR YIAHNGEINT MRGNVNWMQA RQALFESSLF
GEDMAKVQPV INIDGSDSTI FDNALELLYL AGRSLPHAVM MMIPEPWSAH ESMSQEKKAF
YKYHSCLMEP WDGPASIAFT NGKMMGAVLD RNGLRPSRYY VTKDDLVIMA SEAGVLPIEP
ERVAKKGRLQ PGRMFLVDME QGRIIADEEI KQEIVSQHPY GEWLAANLKS LEQLPSPGNV
PGTDAESLRQ RQMAFGYTFE ELRILLAPMG RDGVEAIGSM GADTPLAVLS DKPKLLYNYF
QQLFAQVTNP PIDSIREEII TSAETTIGGE GNLLDPRPES CRLIELKTPI LTNEDLAKLK
ALDDDEFKSV TLDILFDPNQ GEAGLKTALD NLFTEADQAI SQGANLIILS DRQVSAEKAA
IPALLAVSGL HHHLIRNGSR TKVGLVLESG EPREVHHFAV LLGYGCGAIN PYLAFETLDG
MIAEGLLVNV DHKTACKNYI KAATKGVIKV ASKIGISTIQ SYRGAQIFEA VGLNQSVIDE
YFCRTSSRIQ GSDLGVIAQE AILRHQHAFA PRPGDLHTLD VGGEYQWRKD GEEHLFSPQT
IHLLQRAVRE GNYELYKQYA ALVNEQNQKF FTLRGLLDFQ DRESIPLEEV EPIEAIMKRF
KTGAMSYGSI SKEAHESLAI AMNRIGGKSN TGEGGEDPER FTWTNDQGDS KNSAIKQVAS
GRFGVTSLYL SQAKEIQIKM AQGAKPGEGG QLPGKKVYPW IAKVRHSTPG VGLISPPPHH
DIYSIEDLAE LIHDLKNANR EARINVKLVS EVGVGTIAAG VAKAHADVVL VSGYDGGTGA
SPQTSIKHAG LPWELGLAET HQTLVLNNLR SRIVVETDGQ MKTGRDVAIA ALLGAEEFGF
STAPLVSLGC IMMRACHLNT CPVGIATQNP ELRAKFTGDP AHAVNFMTFI ATELREVMAQ
LGFRTINEMV GRTDILEPKK AVAHWKAKGI DLSTILHQPE VGDDVGRYCQ IPQDHGLQHS
LDITQLLDLC QPAIAKGEKV TATLPITNIN RVVGTIVGNE ITKRHWEGLP EDTVHLHFQG
SAGQSFGAFI PKGMTLELEG DANDYLGKGL SGGKIIVYPP KGSSFIASEN IIAGNVCLYG
ATAGEVYISG MVGERFCVRN SGVNTVVEAV GDHGCEYMTG GKVVVLGQTG RNFAAGMSGG
VAYIFDETGD FATRCNSAMV GLEKLEDPEE IKDLKELIQN HVNYTDSAKG KAVLADWEAS
IPKFVKVMPR DYKRVLQAIK KALEAGLSGD DALNAAFEEN AKDVARIGGS
