ID A0A1E5D7V0_9VIBR Unreviewed; 1515 AA.
AC A0A1E5D7V0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OEE79773.1};
GN ORFNames=A130_01470 {ECO:0000313|EMBL:OEE79773.1};
OS Vibrio genomosp. F6 str. FF-238.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE79773.1, ECO:0000313|Proteomes:UP000094165};
RN [1] {ECO:0000313|EMBL:OEE79773.1, ECO:0000313|Proteomes:UP000094165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF-238 {ECO:0000313|EMBL:OEE79773.1,
RC ECO:0000313|Proteomes:UP000094165};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
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}.
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:OEE79773.1}.
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DR EMBL; AJYW02000017; OEE79773.1; -; Genomic_DNA.
DR RefSeq; WP_017051053.1; NZ_AJYW02000017.1.
DR Proteomes; UP000094165; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
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; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF145; GLUTAMATE SYNTHASE, LARGE SUBUNIT; 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 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:UP000094165}.
FT DOMAIN 21..420
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1515 AA; 167564 MW; DF80287404F5F91A CRC64;
MVDQEQNSQG LYTPELEHDA CGIGFVAHLK NRKSHDVVTQ ALDMLARMEH RGGQGCDPCS
GDGAGILLQK PHEFLLEEAV KLGIKLPSFE KYGVGVVLFP KDEHKRAQCR DILERNAQRL
ELEVIGYREL PTDNSMIGAD PLSTEPQFEH VFISGGPGST PEELERKLYV LRNYTVRVCL
ESVSNIGDDF YINSMSYKTV VYKGQLTTEQ VPQYFLDLQN PTMVSALALV HSRFSTNTFP
RWRLAQPFRY IAHNGEINTV RGNLNWMKAR EAIIESDLFT KAEIDMLLPI CQEGSSDSSN
FDMALELLVL SGRSLPHALM MMIPEAWQEN KNMDPTRRAF YQYHANVMEP WDGPASVCFT
DGVQVGATLD RNGLRPSRYT VTKDDFLVMA SESGVVEIEP ENVEFRGRLQ PGRIFVADLE
QGRIISDEEV KDGIANAQPY EKWVEDNLLN LNKLPDAENE FSQPTPEKLL HKQQAFGVSS
EEVNEIIVPM AKDGKEPLSA MGADWPLAIL SHQSQHLSNY FKQLFAQVTN PPIDPIRERM
VMSLNTYLGK DQNLLAESPE HCQKVELESP VLSNSELEKL RAIDNEHLQA KTLDIVFQAS
EDEGKLERAL KRICQYAEDA VIDGYSIILL TDRAVNSNHA AIPAMLAVGA VHHHLIRKGL
RAKCDIVVET GDARETHHFA TLIGYGANAV NPYLVIETMV DLQRTKKLDP QTNIKELFEN
YRNSINGGLL KIFSKMGIST LQSYHGAQIF EALGVSKSVV DKYFTGTVSR IQGLTIDDIA
KEVMVRHRIG YPTREIPVQI LDVGGVYQWK QRGEKHLFNP ETISLLQEST RNKDYGQFKK
YAKAVDDQGD HAATLRSQLD FVKNPAGSIP LEEVEPIEKI LKRFATGAMS FGSISHEAHS
TLAVAMNRIG AKSNSGEGGE DPTRFERKEN GDWERSAIKQ VASGRFGVTS YYLSNADELQ
IKMAQGAKPG EGGQLPGDKV DDWIGATRHS TPGVGLISPP PHHDIYSIED LAQLIYDLKN
ANRNGRVNVK LVSEAGVGTI ASGVAKAKAD VVLIAGFDGG TGASPMSSIR HTGLPWELGL
AETHQTLLKN GLRNRIVVQS DGQMKTPRDL AVATLLGAEE WGVATAALVV EGCIMMRKCH
KNTCPVGIAT QNKTLRERFD GRVEDVVTFF QYMAEGLREV MAELGYRSID EMVGQSHKLK
VRDDIQHWKY KNLDLSPVLH IEQPRAEDGV YNQTQQNHNL EDVLDRKLIQ AAIPALEKGE
AVNAEFPIIN TDRSAGTMLS NEISKVYKDA GLPQPMNVKF NGSAGQSFGA FLAKGVKFEV
EGDANDYWGK GLSGGTLVLY PNAKSSIVAE DNIVVGNVCF YGATSGESYI RGMAGERFCV
RNSGAKVVVE GIGDHGCEYM TGGVAVILGS TGRNFAAGMS GGVAYVWDKA GDFDTKLNPE
LVDLDPIEAE DRELLKEMLT KQVQLTGSEV AQSFLDNFEA SLATMVKVMP RDYKAVLQKR
KTEAEQAQTE EVEAV
//
