ID A0A0B4XFE2_9GAMM Unreviewed; 1487 AA.
AC A0A0B4XFE2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:AJD46769.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AJD46769.1};
GN Name=gltB {ECO:0000313|EMBL:AJD46769.1};
GN ORFNames=S7S_01725 {ECO:0000313|EMBL:AJD46769.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD46769.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD46769.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD46769.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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; CP004387; AJD46769.1; -; Genomic_DNA.
DR RefSeq; WP_041025870.1; NZ_CP004387.1.
DR STRING; 391936.S7S_01725; -.
DR KEGG; apac:S7S_01725; -.
DR HOGENOM; CLU_000422_8_2_6; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000006764; 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: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,
KW ECO:0000313|EMBL:AJD46769.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006764}.
FT DOMAIN 21..410
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1487 AA; 162816 MW; 4F0DD61F870DAA89 CRC64;
MQQNSTLVRG LYEPGEFRDN CGFGLIAHTE GKASHELLQT AIEALTCMTH RGGINADGKT
GDGCGLLLKK PDSFFRKVAA GQGITLPDTY GVGMLFLHPE ADKAAAQRAI VEEELKRQQV
EVYGWRDVPT DPEYLGPIAR ESLPAFAQVL VGVDGLSDVE LNRRLFFARR HAENRVGTDD
YFYVCSLSST VVSYKGLMMP VDLPAFYPDL GDEAMETAIV VFHQRFSTNT MPRWPLAQPF
RYLAHNGEIN TISGNRNWSV ARTPKFVNDL LPGLEDVKPL VNRTGSDSSS MDNMLEILLA
GGMNLFRAVR MMVPPAWQNV ETMDADLRAF YEYNSMHMEP WDGPAGLVMT DGRFAVCMLD
RNGLRPSRWV ITKNGFITLS SEIGVYSYAP EDVVAKGRVG PGQILAVDTE TGELLRTNDI
DNQLKVGQPY RKWLKENGLR IEADYDTEVE RVDEVQPSDL LAYQKLFQVS FEERDQVLRP
LAESGQEAVG SMGDDTPMAV LSKRARPLYD YFRQQFAQVT NPPIDPLREA IVMSLETCIG
AERNVFEETA EHADRAILST PILSHSKFAN LLKIQRPGYA HERLSLHYAP ATGLRQAIVD
LCEKAENAVR AGKVLMVLSD YGIEQDKLTI PAGMATGAVH HRLTEKGLRC DANIIVETAT
ARDPHHFAVL FGFGATAVYP YLAYDVIADM VRSGELLGDA VELQKNFRKG INKGLLKILS
KMGISTIASY RGAQLFEAVG IARDVVDLCF RGVPSRIAGA DFSDFEADFL SLQRDAWKQR
KPIDAGGVLK FIYGKEYHAF NPDVIHALHD AVNSGDYEAY KKYAALVNTR PVATLRDLLR
LRDDVTAISV DDVEPIENIL PRFDSAGMSL GALSPEAHEA IATAMNRLGG RSNSGEGGED
PARFGTERVS KIKQIASGRF GVTPHYLVNA EVLQIKVAQG AKPGEGGQLP GGKVNELIAR
LRYSVPGVTL ISPPPHHDIY SIEDLAQLIF DLKQVNPQAQ VSVKLVSEPG VGTIAAGVAK
AYADLITISG YDGGTAASPL TSIRYAGSPW ELGLTEAHQT LRGNDLRGKI RLQTDGGLKT
GLDVVKAAIL GAESFGFGTV PMVVLGCKYL RICHLNNCAT GVATQRDDLR KEHFIGAPEM
LIHYFTFVAT EVRELLAKLG VKSLADLIGR TDLLERIEGE TERQKKLDLM PILRSDHVPA
DKPQFCQVKR NEPFDKGELA EQMVRDMLPA IENASGGSFH YTITNCNRSL GARLSGEIAR
RHGNLGMEKA PIKVRLVGTA GQSFGVFNAG GLHMYIEGDA NDYVGKGMAG GKLVIRPPTG
SPFKSQETAI IGNTCLYGAT GGKLFAAGSA GERFGVRNSG AHAVVEGAGD HCCEYMTGGC
VTVLGDTGYN FGAGMTGGFA YVLDQNNLFF DRINPELIEL HRISTEPMEA HRSHLRSVLR
EYVEETGSEW GQYILDNFDA MSRKFWLVKP KAASLENLLK STRANPA
//
