ID U3B442_9VIBR Unreviewed; 1512 AA.
AC U3B442;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:GAD80700.1};
GN Name=gltB {ECO:0000313|EMBL:GAD80700.1};
GN ORFNames=VEZ01S_38_00890 {ECO:0000313|EMBL:GAD80700.1};
OS Vibrio ezurae NBRC 102218.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219080 {ECO:0000313|EMBL:GAD80700.1, ECO:0000313|Proteomes:UP000016562};
RN [1] {ECO:0000313|EMBL:GAD80700.1, ECO:0000313|Proteomes:UP000016562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102218 {ECO:0000313|EMBL:GAD80700.1,
RC ECO:0000313|Proteomes:UP000016562};
RA Yoshida I., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y.,
RA Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Vibrio ezurae NBRC 102218.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:GAD80700.1}.
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DR EMBL; BATM01000038; GAD80700.1; -; Genomic_DNA.
DR RefSeq; WP_021714402.1; NZ_BATM01000038.1.
DR STRING; 1219080.VEZ01S_38_00890; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000016562; 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:UP000016562}.
FT DOMAIN 21..420
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 912..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 167439 MW; B26983D2B6B466A6 CRC64;
MLDREQSAQG LYTPELEHDA CGIGFVAHLK NRKSHRVVTQ ALDMLARMEH RGGQGCDPCS
GDGAGILLQK PHEFLLEETV KLGIRLPSFE QYGVGVVLFP RDEHKRAQCR DILERNAQRL
DLEVLGYRVL PTDNSMLGAD PLSTEPQFEH VFITGGPSTT PEELERKLYV LRNYTVRVCL
ESVSNIGDDF YINSLSYKTL VYKGQLTTEQ VPQYFLDLQN PTMVTALALV HSRFSTNTFP
RWRLAQPFRY IAHNGEINTV RGNLNWMKAR EAILESDLFS QAEIDMLLPI CQEGSSDSSN
FDMALELLVL SGRTLPHALM MLIPEAWQEN KNMDPKRRAF YQYHANIMEP WDGPASVCFT
DGVQVGATLD RNGLRPSRYT VTKDNFLVMA SESGVVEIEP ENVEFRGRLQ PGRIFVADLE
QGRIISDEEV KDSIANAQPY EAWVEENLLS LKKLPDAENE FNQPSPERLL HKQQSFGVSS
EEVNEIIVPM AKDGKEPLSA MGADWPLAIL SHQSQHLSNY FKQLFAQVTN PPIDPIRERM
VMSLNTYLGK DQNLLTETPE HCQKVELESP VLSNSELEKL RAIDNEHLQS KTLDIVFQAS
EDKGKLERAL KRICQYAEDA VVDGYSIILL SDRAVNSNHA AIPAMLAVGA VHHHLIRKGL
RAKCDIVVET GDARETHHFA TLIGYGANAV NPYLVIETLV DLQRTKKLDP EAHVKELFEN
YRKGVNGGLL KIFSKMGIST LQSYHGAQIF EALGVSKSVV DKYFTGTVSR IQGLTIDDIA
KEVIVRHRIG YPTREIPVQL LDVGGVYQWK QRGEKHLFNP ETISLLQQST RNKDFDQFKQ
YTQAVDRQGD DAATLRSQLD FVKNPAGSIP LEEVEPIEAI LKRFATGAMS FGSISYEAHS
TLAVAMNRIG AKSNSGEGGE DPSRFERKEN GDWERSAIKQ VASGRFGVTS YYLTNSEEIQ
IKMAQGAKPG EGGQLPGDKV DDWIGATRHS TPGVGLISPP PHHDIYSIED LAQLIYDLKN
ANRSGRVNVK LVSEAGVGTI ASGVAKAKAD VVLIAGFDGG TGASPMSSIR HTGLPWELGL
AETHQTLLKN GLRNRIVVQS DGQMKTPRDL AVATLLGAEE WGVATAALVV EGCIMMRKCH
KNTCPVGIAT QNKTLRERFD GRVDDVVTFF QYMAEGLREI MAELGFRTIQ EMVGQSQKLK
VREDIGHWKY KNLDLSPVLH IEPARAEDGV FNQIEQNHNL EEVLDRKLIQ TAIPALEKGE
SVTAEFPIIN TDRSVGTMLS NEISKVYKDQ GLPEPMNVKF NGSAGQSFGA FLAKGVKFEV
EGDANDYWGK GLSGGTLVLY PDANSNIVPE DNIVVGNVCF YGATSGESFI RGLAGERFCV
RNSGAKVVVE GVGDHGCEYM TGGIAIILGS TGRNFAAGMS GGIAYVWDKD GDFETKLNSE
LVDIDPIEAE DKALLQDMLT KHVQFTGSEV AQSFLDNFEV NLQSLAKVMP RDYKAVLQKN
KAAQQQTEAE AV
//
