GLTB_CYACA
ID GLTB_CYACA Reviewed; 1549 AA.
AC O19906;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ferredoxin-dependent glutamate synthase;
DE EC=1.4.7.1;
DE AltName: Full=Fd-GOGAT;
GN Name=gltB;
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF022186; AAB82683.1; -; Genomic_DNA.
DR PIR; T11974; T11974.
DR RefSeq; NP_045078.1; NC_001840.1.
DR AlphaFoldDB; O19906; -.
DR SMR; O19906; -.
DR GeneID; 800212; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00691.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW 3Fe-4S; Amino-acid biosynthesis; Chloroplast; FAD; Flavoprotein; FMN;
KW Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Plastid.
FT CHAIN 1..1549
FT /note="Ferredoxin-dependent glutamate synthase"
FT /id="PRO_0000170791"
FT DOMAIN 37..435
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 37
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1116..1173
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1169
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1175
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1180
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1549 AA; 172012 MW; 6C0965E071453CB4 CRC64;
MISISKRTSI ARINLSEFHT ISKIDRYPWL NKEKDACGVG FIAHLDNKFG HKLMMNALEA
LATMEHRGAC SADEESGDGA GILFSIPWKF FVEWSLRYKQ FKINISQAAV AMLFLPCLSS
DIQVSKNIVE EIFQDEDFIV IGWREVPYVK EVLGPLALRN MPQIYQIVVQ SKRYQGRSLD
FHLYRVRRKI EKEITVRAYS WAKDFYFCSC SNHTIVYKGM VKSTSLGQFY QDLYNPDFEI
SFAVFHRRFS TNTMPRWPLA QPMRILGHNG EINTLLGNLK WMEARESSLN HPTLNEVASI
GPVVNVSNSD SANLDSVVEL FLHVGHSCPE ALMFLIPEAY ENNPKLKYHQ NLISFYEYCA
GFQEAWDGPA LIVFSDGHTV GASLDRNGLR PARYCVTEDN VLILASEGGV LNLDPSLIRL
KGRLGPGEMI VLDLQEKLLM SNLEIKNKIA SLRPYSDWIK QNRQVLIPTS FLTSTTLPLQ
EVFKRQTCFG YTSEDIELVI ENMAIQGKEP TFCMGDDTPL AVLSGKSHVL YDYFKQRFAQ
VTNPPIDSLR ESLVMSISSY LGSKTNSFEE SSEKILKIKT PILSENDLVL IKNSELLTET
LVTTFEAHFD SPQANGQSLF STINQLCKQA KNLIQAGTKI IILSDKVCFE SRTESYIPPL
LVVGSLHQYL IKQGVRQKVS LIVETGQCWS THHFACLLGY GASAVCPYLA LETVRHWWMS
ERTQNLMSKG KMPNLTLIEV QNNYCKSVER GLLKILSKMG ISLLTSYIGA QIFEILGLGK
EVVDLAFEGT VSRIGGLSFA DLAMETIDLC SAGFSKLNKK KLDNHGFVQY RPGGEYHLNN
PEMSKALHKA VRENNYTLYE AYKQLLANRP PTNIRDLLEF NFRSCSVPLE KVENIFEITK
RFCTGGMSLG ALSREAHETL SIAMNRIGGK SNSGEGGEDS LRFTVLTDVD ETGNSPSFPH
LKGLKNGDSL SSAIKQIASG RFGVTPEYLV NAKQLEIKIS QGAKPGEGGQ LPGKKVSPYI
ATLRACKPGV TLISPPPHHD IYSIEDLAQL IFDLHQVNPE CKVSVKLVSE IGVGTIAVGV
AKAGAEIIQI SGHDGGTGAS PLSSIKHAGV PWELGLHEVH CLLVENNLRE KVILRVDGGL
RTGQDVVMAA LLGADEYGFG TIAMIAGGCI MARVCHTNSC PVGVATQKEE LRMRYPGVPE
NVVNYFIFLA EEIRVILSKL GFETLSQIIG RKDLINHNFD KKLCKTHCID TSIFFNIKTN
EYNFLEIPGG HSKKLKTSLL DYELLNSSDI LYAIDNHKTL EKHIKISNSD RSVGAKLAGR
LAKQYKNEGF RGSLILNFYG TAGQSFGSFN IKGVTLRLIG EANDYVGKSM SGGEIVIVPP
SEVAFDASEQ VILGNTCLYG ATGGFLFAYG AAGERFAVRN SNAFSVLEGV GDHACEYMTG
GRVVVLGKAG RNIAAGMTGG IAYFLDEYSN LPEKVNLDIV RIQRVVTNEA RKQLIQLIEK
HVLKTGSKKA VLILQQWEIF IHYFWQIVPP SESETSETNY FVENKVLAN
