ID A0A370HGW9_9HYPH Unreviewed; 1572 AA.
AC A0A370HGW9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Glutamate synthase [NADPH] large chain {ECO:0000256|ARBA:ARBA00072108};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
DE AltName: Full=Glutamate synthase subunit alpha {ECO:0000256|ARBA:ARBA00079921};
GN ORFNames=DES45_10753 {ECO:0000313|EMBL:RDI57138.1};
OS Microvirga subterranea.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Methylobacteriaceae; Microvirga.
OX NCBI_TaxID=186651 {ECO:0000313|EMBL:RDI57138.1, ECO:0000313|Proteomes:UP000254925};
RN [1] {ECO:0000313|EMBL:RDI57138.1, ECO:0000313|Proteomes:UP000254925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14364 {ECO:0000313|EMBL:RDI57138.1,
RC ECO:0000313|Proteomes:UP000254925};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH
CC + H(+); Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00048151};
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; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037898}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDI57138.1}.
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DR EMBL; QQBB01000007; RDI57138.1; -; Genomic_DNA.
DR RefSeq; WP_114771377.1; NZ_QQBB01000007.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000254925; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019676; P:ammonia assimilation cycle; IEA:TreeGrafter.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR FunFam; 3.20.20.70:FF:000031; Glutamate synthase 1 [NADH]; 1.
DR FunFam; 3.20.20.70:FF:000053; Glutamate synthase large subunit; 1.
DR FunFam; 2.160.20.60:FF:000001; Glutamate synthase, large subunit; 1.
DR FunFam; 3.60.20.10:FF:000001; Glutamate synthase, large subunit; 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; IPR050711; ET-N_metabolism_enzyme.
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 NCBIfam; NF008730; PRK11750.1; 1.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 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 Reference proteome {ECO:0000313|Proteomes:UP000254925}.
FT DOMAIN 48..447
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 944..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1572 AA; 172270 MW; 08463C44E2394301 CRC64;
MSDVSNKRLE IEASTRAAAK TDTALVVRDP ALPKLQGLYD PGNEQDSCGV GFIADMKNRK
SHAIVEQGLQ ILLNLDHRGA VGADPKTGDG CGILVQIPHK FFAAECAKLG IWLPDAGEYG
VGHLFMPRDP EGFALVQEIV TKAITDEGLQ VLGWRDVPVD SSDLGESVKA SEPQHRQIFI
GKGKGMDDQE TFERRLFIAR KVISNAVYDM KDPRTAGYYP VSLSSRTIVY KGMVLVGQLG
GYYKDLQDPR FESAIALVHQ RFATNTFPTW QLAHPYRMVA HNGEINTLRG NVNWMAARQA
SVDSDLFGND ISKLWPISYE GQSDTACFDN ALEFLVRGGY SLAHAMMMLI PEAWAGNPLM
DEDRRAFYEY HAALMEPWDG PAAVCFTDGK QIGATLDRNG LRPARYLVTE DGLVVLASEM
GVLPIPEEKI VEKWRLQPGK MLLIDLEEGR IVSDDEIKQQ LSQAHPYKDW LKRTQIVLED
LKPVQARESR TDVSLLDRQQ AFGYTAEDLK LLMQPMAVTG QEAVGSMGSD TPISALSDKP
KLLYTYFKQN FAQVTNPPID PIREELVMSL VSFIGPRPNI LDLEGTSRRK RLEVRQPILT
NEDLEKIRCI GHFEDRFDTK TLDITYPSEL GAAALDGALD RLCDRAEAAV HGGYNIIILS
DRMVGPDRIP IPALLATAAV HNYLIRKGLR TSVGLVLESG EPREIHHFAC LAGYGAEAIN
PYLAFETIAA MHAAGELPGE VDEDEAIKRY IKSIGKGLLK VMSKMGISTY QSYCGAQIFD
AVGLRSDFVN RDFFGTATTI EGIGMDEVSE ETVRRHRDAF GDAPVYRDAL DVGGEYAYRT
RGEVHAWNPD TVATLQHAVR LNAQDRYREY ARLVNEQEHE LKTIRGMFRI KMAEEADRAP
VSLDEVEPAA EIVRRFSTGA MSFGSISKEA HETLALAMNA IGGKSNTGEG GEEPERFRQL
PDGRSKRSAI KQVASGRFGV TTEYLVNADM MQIKIAQGAK PGEGGQLPGH KVDAKIARVR
HSTPGVGLIS PPPHHDIYSI EDLAQLVFDL KNVNPSADVS VKLVSEVGVG TVAAGVAKAR
ADHITISGFE GGTGASPLTS LKHAGSPWEI GLAETQQTLV LNRLRGRVAL QADGGLRTGR
DVVIAALLGA DEYGFSTAPL IAAGCIMMRK CHLNTCPVGV ATQDPVLRKR FKGLPEHVIN
YFFFVAEEVR EMMAAMGFRT IDEMIGRSEL LDKNGAIDHW KAKGLDFTRI FHKPEVGPDV
PVRHVERQVH PIAEVLDRSL IAEAGPALEQ GEAVTIEARV RSADRAVGAM LSGEVAKRYG
HEGLPDDTIT VKLKGTAGQS FGAWLAAGVT LALEGEANDY VGKGLSGGKL IIRPSPDSKA
VPERSIVVGN TVMYGAIAGE AYFRGVAGER FAVRNSGAIA VVEGTGDHGC EYMTGGLVVV
LGQTGRNFAA GMSGGIAYVL DEDGTFAKRC NLSMVDLEPV EEEEDLMRRL HHHGGDLETK
GRIDIMANMS GPDEERLMQL ITNHHTYTGS ARAKEILDHW TTYRTKFVKV MPVEYRRALQ
EMDRLRTLQA AE
//
