ID A0A1Z9VZ91_9GAMM Unreviewed; 1482 AA.
AC A0A1Z9VZ91;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:OUX70706.1};
GN ORFNames=CBC51_03355 {ECO:0000313|EMBL:OUX70706.1};
OS Oceanospirillales bacterium TMED91.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX NCBI_TaxID=1986769 {ECO:0000313|EMBL:OUX70706.1, ECO:0000313|Proteomes:UP000196344};
RN [1] {ECO:0000313|EMBL:OUX70706.1, ECO:0000313|Proteomes:UP000196344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED91 {ECO:0000313|EMBL:OUX70706.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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:OUX70706.1}.
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DR EMBL; NHES01000025; OUX70706.1; -; Genomic_DNA.
DR Proteomes; UP000196344; 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..405
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1482 AA; 161124 MW; D94EC6FEA811CB1C CRC64;
MTKGLYTPGE FRDNCGFGLI AHCDGEXSHD LLMTSIEALT RMTHRGGIAA DGKTGDGCGL
LFQMPEAFMR HAASEACGVE LGDLFAVGMV FLSTDPSVEA XAVSAIEAVL NSRRLAVIGW
RNVPVDPSNL GPIARGNMPV FKQVFVEPQG QNKEQFDNEL FMASRLIERR MASNSDNYLC
SLSRRVVSYK GLMMPVDLHH FXPDLNDPLM ATAICVFXQR FSTNTLPRWP LAQPFRLLAX
NGEINTIAGN RNWANARGHL XTSARLPEID QILPLVNSTG SDSSSLDNML EVMVAGGMDL
FRAIRMLVPP AWQNVDDMDA DLRAFYEYNS MHMEPWDGPA GIVLTDGRYA CCLLDRNGLR
PARWVKTKNG YLTLASEIGT WDYKPEDVIA KGRVGPGEIL AIDTETGEML SADDIDHQLK
GRQPYKQWLR EQTIRFEADM KDPFSDLKQL SEKGLAPYLK XFNLTSEERH QVIKPLAETG
QEAVGSMGDD TPMAVLSTEQ RHVADYFRQQ FAQVTNPPID PLRESIVMSL ETCLGMELNP
FEETADHAER VILHSPILSA PKMDRLKALE HPKYGRIQIE LAFDPAMGLK AAVESVCQQA
VDAARSGKTL LILSDRHVAE HQWVVSATIA TGAVHHRLIA EGLRCSANII VDTAEARDSH
QFAVLLGFGA TAVYPYLSYR VINDLVDSDE LVGDSLELHR NYRKGINKGL LKILSKMGIS
TVASYRGAQL FEAVGLSNEI VDLCFKGVQS RIAGADFSDF ENDQKIRQSL AWSTRKPVPQ
GGFLKYMHGG EYHAYNPDVV QTLQQAVQTG SYSTYQKYAK LVNDRPVATL RDLLKLEKDA
GRAXTVDEVE PIESILKRFD SAGMSLGALS PEAHEALAQA MNELGARSNS GEGGEDPDRF
GTSRTSKIKQ IASGRFGVTP HYLVNAEVLQ IKVAQGAKPG EGGQLPGGKV XALIARLRHS
VPGVTLISPP PHHDIYSIED LAQLIFDLKQ VNPKALVSVK LVSEPGVGTI AAGVAKAYAD
LITISGYDGG TAASPLTSIK YAGSPWELGL AEAHQALRAN DLRDKVRXQT DGGLKTGLDV
XKAAIXGAES FGFGTAPMVA MGCXYLRICH LNNCATGVAT QNELLRXQHF RGTVEMIKHF
FTFVAEETRE VMAELGVKTI AELVGRTDLL TQVGGRSQRQ AKLDFSPILY QGPEHEGKXQ
LCAVEKNPPY DDAPLNXAIV HAARDGMXSG EGGEFHXTIT NQDRSVGATL SGEISLAHGR
EGMAXPIRLN LEGTAGQSFG VFNAPGLEMX LRGDANDYVG KGMAGGRLAI APPEGSTFAS
QDTSIIGNTC LYGATGGTLY AAGRAGERFA VRNSGATAIV EGTGDHCCEY MTGGLVIVLG
RTGRNFGAGM TGGFAYVLDE SRTFVDRYNH ELVEIARIST EQMEQYRAHL RSQIRDYAEA
TGSAWGQTIL SDFESSVSHF WLVKPKAASL GDLLASSRSD AQ
//
