GLTB_HALED
ID GLTB_HALED Reviewed; 1482 AA.
AC E1V8I1;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Glutamate synthase [NADPH] large chain {ECO:0000250|UniProtKB:P09831};
DE EC=1.4.1.13 {ECO:0000269|PubMed:28081159};
DE AltName: Full=GOGAT {ECO:0000303|PubMed:28081159};
DE AltName: Full=Glutamate synthase subunit alpha {ECO:0000250|UniProtKB:P09831};
DE Short=GLTS alpha chain {ECO:0000250|UniProtKB:P09831};
GN Name=gltB {ECO:0000303|PubMed:28081159};
GN OrderedLocusNames=HELO_3753 {ECO:0000312|EMBL:CBV43637.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=28081159; DOI=10.1371/journal.pone.0168818;
RA Kindzierski V., Raschke S., Knabe N., Siedler F., Scheffer B.,
RA Pflueger-Grau K., Pfeiffer F., Oesterhelt D., Marin-Sanguino A.,
RA Kunte H.J.;
RT "Osmoregulation in the halophilic bacterium Halomonas elongata: a case
RT study for integrative systems biology.";
RL PLoS ONE 12:E0168818-E0168818(2017).
CC -!- FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate
CC into two molecules of L-glutamate. {ECO:0000269|PubMed:28081159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; 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:0000269|PubMed:28081159};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P09831};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P09831};
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:0000250|UniProtKB:P09831}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000250|UniProtKB:P09831}.
CC -!- INDUCTION: Up-regulated at high salt concentration.
CC {ECO:0000269|PubMed:28081159}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; FN869568; CBV43637.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V8I1; -.
DR SMR; E1V8I1; -.
DR STRING; 768066.HELO_3753; -.
DR EnsemblBacteria; CBV43637; CBV43637; HELO_3753.
DR KEGG; hel:HELO_3753; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_6; -.
DR OMA; TVFRLQH; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00689.
DR Proteomes; UP000008707; Chromosome.
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: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 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; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..1482
FT /note="Glutamate synthase [NADPH] large chain"
FT /id="PRO_0000439539"
FT DOMAIN 15..405
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 1049..1101
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1102
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1108
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1113
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1482 AA; 162155 MW; 4BCFC4DE052EB6FA CRC64;
MNRGLHQPDE FRDNCGFGLI AHMEGQASHD LLKTAIESLT CMTHRGGIAA DGKTGDGCGL
LLKMPESFMR EVAREALGVE LGERFAVGSI FLPDDDAREA QGRETLEAEL TKRGLNVLGW
REVPVDPSVC GPMALDCLPR IRQLFVEPGE ETGDTFDVDL FMARRHAEQA LRDEEDFYVC
SLSPEVVSYK GLVMPVDLPA FYHDLGDTRL ETAICVFHQR FSTNTAPRWP LAQPFRLLAH
NGEINTIQAN RGWANSRKEN FTSERLPDIA ELDEIVNTTG SDSSSMDNML EVLLTGGMDL
HRAVRMMVPP AWQNVEIMDG DLRAFYEYNS MHAEPWDGPA GVVMTDGRQA VCMLDRNGLR
PARWVITRNG YITLASEIGT YDYRPEDVVA KGRVGPGQIL AVDTETGEVL HTEDIDSRLK
SAYPYKRWLK QEASYLESAL TELARFQNMD ADTLAVQQKM FQISFEERDQ ILRPLAESGQ
EGVGSMGDDT PMAVLSTKQR LLTDYFRQKF AQVTNPAIDP LREAIVMSLE SCIGAELNVF
KATPEHAHRL ILTTPVLSPR KFTALVTQED PAFASQTLSL AYDPETTGLK DALQALCAEA
EKAARGDKVL LVLSDANLEK GQLPIHAALA VGAVHHHLGR LALRPRVNLI VETGYARDAH
QMAVLFGVGA TAVYPWLAYQ VMADMHRTGE LVGNPADARE NYRKGLQKGL FKILSKMGIS
TLASYRGSQL FEAVGLASEV MDMCFTGMAS RIEGTGFAEL QLQQELLAKD AWKPRKSISH
GGLMKYVHGH EYHAYNPDVI KALQEAVQEG DYTKWKKFAA LVNERDPATI RDLLRLKPAE
TPVPLEEVEP VENLLPRFDS AGMSLGALSP EAHEALAQAM NETGGRSNSG EGGEDPVRYG
TIRSSKIKQI ASGRFGVTPA YLANAEVLQI KVAQGAKPGE GGQLPGGKVN ELIARLRYAV
PGVTLISPPP HHDIYSIEDL AQLIFDLKQV NPDAQVSVKL VSEPGIGTIA TGVAKAYADL
ITVSGYDGGT AASPLTSIKH AGSPWELGLP EVHQALRING LRDKIRLQTD GGLKTGLDVI
KAAILGAESF GFGTAPMVAL GCKYLRICHL NNCATGVATQ HQVLRDEHFR GTVDMVKHYF
RFIAEEVREL MAMLGVRQLT DLIGRTDLLE AIEGVTPSQR RLDLSPLMTN DFVPAEAPQF
CQVDRNVPHD PGAKNQEVLA AMKTAIEQKS GGEFEFAITN CDRSVGALAS GTIAKRYGEA
GLEDAPVTAR FRGVAGQSFG VWNARGLHLY LEGDANDYVG KGMNGGRVVI VPPRESRFES
HKTAIIGNTC LYGATGGKLF ASGTAGERFG VRNSGAQAVI EGAGDHCCEY MTGGLVAVLG
ETGVNFGAGM TGGFAYVLDE DRTFVDKYNH ELVEIHRVNT EAMEAHRRHL REVIEEFVAE
TGSQRGRDIL EDFSDFIRHF WLVKPKAASL ASLLDQSRRQ PE
