ID A0A165SNX6_9GAMM Unreviewed; 1479 AA.
AC A0A165SNX6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:KZX56098.1};
GN Name=gltB {ECO:0000313|EMBL:KZX56098.1};
GN ORFNames=A3709_06850 {ECO:0000313|EMBL:KZX56098.1};
OS Halioglobus sp. HI00S01.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Halioglobus.
OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX56098.1, ECO:0000313|Proteomes:UP000077184};
RN [1] {ECO:0000313|EMBL:KZX56098.1, ECO:0000313|Proteomes:UP000077184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX56098.1,
RC ECO:0000313|Proteomes:UP000077184};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-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:KZX56098.1}.
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DR EMBL; LWEE01000215; KZX56098.1; -; Genomic_DNA.
DR RefSeq; WP_066057227.1; NZ_LWEE01000215.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000077184; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077184}.
FT DOMAIN 15..405
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1479 AA; 161650 MW; C7DC3354FAD3F3A0 CRC64;
MNAGLYRPEE FRDNCGFGLI AHTSGEASHR LLQTAIESLT CMTHRGGIAA DGKTGDGCGL
LLQMPRQFMA TLAQELFGAT LSDMFAVGQI FLSRDAEAAQ AARAATEVAL TDQGLTVIGW
REVPTDDSVC GEIALETLPR IEQVFIDAAG LTDVELSTKL FVARRKAEMA CEQDEDYYIA
SLSGRVISYK GLVMPVDLPK FYQDLADERL ETAICVFHQR FSTNTMPKWP LAQPFRLLAH
NGEINTIEGN RNWAEARTAC FETERLPNIK DIAPLVNRTG SDSSSMDNML DVLLTGGVDM
ARALRMLIPP AWQNMELMDP DLKAFYEYHS MHMEPWDGPA GLVLTDGRYA VCMLDRNGLR
PARWVKTKDG FITLASEIGT YDYKPEDVVA KGRVGPGQMM MVDTQTGELL QTEDIDNRLK
NAQPYKRWLK EKAQRIEGTF GSEMISGIER AQLDAYMKMF QVSFEERDQV LRPLAESGNE
AVGSMGDDTP MAVLSRKERS LYDYFRQKFA QVTNPPIDPL RETIVMSLET DLGGEKNLFH
EGPEHADRVI LTSPVLSQGK FTTLLNLDRP GFQPRKIDCT YNPDEMSLEQ GVRQVIAEAE
SAVNSGSTIL VLSDREIEKG RLPIHSMLTT GAVHHALIKL GLRAECNIVV ETASARDSHQ
IACLLGFGAT AVYPYLAYSV LEELIRCGEV LGEPSICYKN YRKGINKGLL KIMSKMGISA
VSSYRGAQLF EAVGLAREVV DLSFCGVASR IEGSGFSELE AEQQLLAKRA WTPRKTIEQG
GLLKYVHGQE YHAYNPDVVM SLQQAVASGD YADYQRYAAL VNERPVATLR DLLRPVEGAG
IDINEVEPVE NILPRFDSAG MSLGALSPEA HEALAAAMNR MGARSNSGEG GEDPIRYGTE
RMSKIKQIAS GRFGVTPHYL VNAEVLQIKV AQGAKPGEGG QLPGGKVNDL IARLRYSVPG
VTLISPPPHH DIYSIEDLAQ LIFDLKQVNP DALVSVKLVS EPGVGTIAAG VAKAYADLIT
ISGYDGGTAA SPLTSIRYAG SPFELGLAEV QQTLRGNNLR GAIRLQADGG LKTGLDVIKA
AILGAESFGF GTGPMVALGC KYLRICHLNN CATGVATQHQ KLRDDHFNGT VEMVMNFFTF
IAMETREWLA RLGVRSLEEL IGRTDLLEAL PGDTDKQTRL DLAPILHKDD DAAGQPEFCQ
VSSNDPFDKG EKAEEMVAAT LANIEANQGG EFAFEVCNCD RSIGARLSGE IAKRYGNEGM
ETNPLVLRLT GTAGQSFGVW NAGGLHMYLE GDSNDYVGKG MAGGKLVIYP PRVSEFKSQE
TSIIGNTCLY GATGGRLFAA GIAGERFAVR NSGAHAVVEG AGDHCCEYMT GGNVTVLGPT
GVNFGAGMTG GFAYVLDMDR TFIDKYNSEL VEIHRVSAEY MEPYRNHLRG NIREFVEETG
SEWGTHLLDN FEDYVGKFWL VKPKAAEFDA LLSRLRNTD
//
