ID A0A193K9W5_9VIBR Unreviewed; 1487 AA.
AC A0A193K9W5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:ANO32095.1};
GN ORFNames=A6E01_02180 {ECO:0000313|EMBL:ANO32095.1};
OS Vibrio breoganii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=553239 {ECO:0000313|EMBL:ANO32095.1, ECO:0000313|Proteomes:UP000092018};
RN [1] {ECO:0000313|EMBL:ANO32095.1, ECO:0000313|Proteomes:UP000092018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF50 {ECO:0000313|EMBL:ANO32095.1,
RC ECO:0000313|Proteomes:UP000092018};
RA Hehemann J.-H., Arevalo P., Datta M.S., Yu X., Corzett C., Henschel A.,
RA Preheim S.P., Timberlake S., Alm E.J., Polz M.F.;
RT "Adaptive Radiation by Waves of Gene Transfer Leads to Fine-Scale Resource
RT Partitioning in Marine Microbes.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; CP016177; ANO32095.1; -; Genomic_DNA.
DR RefSeq; WP_017026863.1; NZ_MDAV01000039.1.
DR STRING; 553239.A6E01_02180; -.
DR KEGG; vbr:A6E01_02180; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000092018; Chromosome 1.
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: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 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}.
FT DOMAIN 13..403
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1487 AA; 163061 MW; A10EB1B68ACDA779 CRC64;
MALYDPSLER DNCGFGLIAH MEGEASHKLV RTAISALDRM THRGGIAADG KTGDGCGLLL
QKPDSYFRMI AQEQQWNLGK QYAVGMFFLS RDPVISQQCK AAINKELGQE TLSVEGWRTV
PTNSDVLGPI ALESLPSIEQ VFVSAPAGWS EKDIERRLYI ARRRIEKALS EQQDFYICSL
STKVIVYKGL CMPADLPRFY LDLADLRLES AICLFHQRFS TNTQPRWPLA QPFRYLAHNG
EINTIQGNRQ WAKARAYKFS SPLLPDLQTA APFVNETGSD SSSLDNMLDL FLAGGMDIFR
AMRMLVPPAW QNHPDMDPDL RAFYDFNSKH MEPWDGPAGI VLSNGRYAAC NLDRNGLRPA
RYVITKDKLI TLASEVGIWD YAPDEVSEKG RVGPGELLVV DTKEGKLWHS DEIDNDLKSR
HPYREWMENN VHKLTPFSDL SGDEIGQRSL SNDELKTYQK QFAFSREERE QVLKVLGDMG
QEAVGSMGDD TPMAVLSSRE RLVTDYFRQK FAQVTNPPID PLREKHVMSL ATSVGKEMNV
FNETDGHAYR VTFDSPVLLY SDMQQLLELN QKHYKHQYFN LCYSPDELSL EQAIRALCDA
SEQAVRDGAV LLVLSDRNLE KGKLPIPAAM AVGAVQNRLV EAQLRCDTNI IVKTATARDP
HQFAVLFGFG ATAVYPYLAY EILAEQIDNG GIDKPYAEVM LNYRKGIDKG LFKIMSKMGI
STIASYRCSQ LFEAVGLHQD IIELCFKGVS SRIQGAHFDD FQQDLFNLSR KAWAKRKDIE
HGGLLKYVHG GEYHTYNPDV VSQLQTAVKT GENQDYQTYA NQVNQRPIST LRDLMQLKKA
PQPLANEQVE PAKELFKRFD SAAMSIGALS PEAHQALAQA MNHLGGYSNS GEGGEDPSRF
GTNRNSRIKQ VASGRFGVTP HYLTNADVLQ IKVAQGAKPG EGGQLPGHKV TAEIAKLRHS
VQGVTLISPP PHHDIYSIED LAQLIFDLKQ VNPDALVSVK LVSEPGVGTI ATGVAKAYAD
LITISGYDGG TAASPLTSVK YAGSPWELGL AETQQALVAN GLRHKIRLQV DGGLKTGLDV
IKGAILGAES FGFGTAPMVA MGCKFLRICH LNNCATGVAT QDETLRKEYF KGLPEMVINY
FTGLAEEVRG YLAELGVEKL TDLIGRTDLL EVVEGFTAKQ SKLDLSDILE TPVSPTGAPV
FWSEPNKPFD KAFLNQTIVE EALAAVEAKA PLNLYYDVKN TDRSIGARLS GEIAKRYGNA
GVAGSPICLN LNGTAGQSLG VWNAGGVNIK LTGDANDYVG KGMAGGKISI RPHLGSAFES
QQAAIIGNTC LYGATGGKLF AAGRAGERFA VRNSGTIAVV EGAGDNACEY MTGGIVAILG
ATGVNFGAGM TGGFAYVFDH NQDFQGRVNQ ESVEAISLES LVIHQEHLRG LIAEHLEETA
SSHAEAILAN FDHWIPRFYL IKPKAADLNT LLGHQSRSAA ELRVQAQ
//
