ID A0A1J8PZC1_9GAMM Unreviewed; 1480 AA.
AC A0A1J8PZC1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:OJA06841.1};
GN ORFNames=QHL1GM_16300 {ECO:0000313|EMBL:OJA06841.1};
OS Halomonas sp. QHL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1123773 {ECO:0000313|EMBL:OJA06841.1, ECO:0000313|Proteomes:UP000183854};
RN [1] {ECO:0000313|EMBL:OJA06841.1, ECO:0000313|Proteomes:UP000183854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QHL1 {ECO:0000313|EMBL:OJA06841.1,
RC ECO:0000313|Proteomes:UP000183854};
RA Seilhamer J.J.;
RL Submitted (AUG-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}.
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:OJA06841.1}.
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DR EMBL; MINL01000001; OJA06841.1; -; Genomic_DNA.
DR RefSeq; WP_071695434.1; NZ_MINL01000001.1.
DR STRING; 1123773.QHL1GM_16300; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000183854; 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: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 15..403
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1480 AA; 160998 MW; 7F3279E4D39565B1 CRC64;
MNRGLHQPGE FRDNCGFGLI AHMEGQASHD LLKTAIESLT CMTHRGGIAA DGKTGDGCGL
LLKMPTPFMQ ALAKEAFDAE LGERFAVGVV FLPDDDARET HARDTLTFEL EARGLNVVGW
RDVPTDSSVC GPMALDCLPR IRQLFVQPGQ GEHFDVDLFM ARRRAEQVLR DEEDFYVASL
SSEVISYKGL MMPEDLPAFY KDLNDPRLET AICVFHQRFS TNTAPRWPLA QPFRLLAHNG
EINTIEANRG WANSRKANFV NERLPDIAEL DEIVNTTGSD SSSMDNMLEV LLTGGMELHR
AVRMMVPPAW QNVETMDAEL RAFYEYNSMH MEPWDGPAGV VMTDGRQAVC MLDRNGLRPA
RWVITKNGYI TLASEIGTYG YKPEDVVAKG RVGPGQMLAV DTETGEVLHT SDIDERLKSA
YPYKRWLKQE ASYLESALTE LARFQSMDTD ALNVQQKMFQ VSFEERDQVL RPLAESGQEA
VGSMGDDTPM AVLSSRPRLL TDYFRQKFAQ VTNPAIDPLR EAIVMSLETC CGAELNVFKA
TPEHAHRLIL TTPVLSPRKF TALVSQDDPA FASHTMSLGY DPEQQSLHQA LKALCEDAEA
KVRAGKVILV LTDAELSKGL IPIQAALAVG AVHSHLGRLA LRPNANIVVE TGYARDAHQM
AVLFGVGATA VYPWLAYQVM ADMHRTGELT GNPADGRENY RKGLQKGLFK ILSKMGISTL
ASYRGSMLFE AVGLADEVMD MCFVGMASRI QGTGFAELQM QQALLAKDAW IPRKGISQGG
MFKYVHGHEY HAYNPDVVMS LQAAVQEGSY TKWKKFAQLV NERPVATIRD LLKLKTVETP
IALDEVEPVE ELLPRFDSAG MSLGALSPEA HEALAQAMNE AGGRSNSGEG GEDPSRYGTI
RSSKIKQIAS GRFGVTPAYL VNAEVLQIKV AQGAKPGEGG QLPGGKVNQL IARLRYAVPG
VTLISPPPHH DIYSIEDLAQ LIFDLKQVNP DAQVSVKLVS EPGIGTIATG VAKAYADLIT
VSGYDGGTAA SPLTSIKHAG SPWELGLPEV HQALRINGLR DKIRLQTDGG LKTGLDVVKA
AILGAESFGF GTAPMVALGC KYLRICHLNN CATGVATQDD FLRGEHFRGT VDMVKNYFRF
IAEEVRELMA ALGVRKLTDL IGRTDLLEVL EGNTASQRKL DLTPLLANDF VPKDAPQFCT
VSRNVPHDPG AKNQEVLAAL KDAIESQSGG EFDFTITNCD RSVGALSSGA IAKRYGEEGL
EAAPVTANFV GVAGQSFGVW NARGLNLFLE GDANDYVGKG MNGGSIVIVP PKVSQFESHK
TAIIGNTCLY GATGGTLFAA GTAGERFAVR NSGASAVIEG AGDHCCEYMT GGLVCVLGET
GVNFGAGMTG GFAYVLDEER TFVDKYNHEL VEIHRVNTEA MEAYRRHLRE MIEAYVAATG
SARGAAILED FSDYARHFWL VKPKAASLGS LLDQSRRQPQ
//
