ID A0A1F1QG10_9PSED Unreviewed; 1481 AA.
AC A0A1F1QG10;
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:OFS76205.1};
GN Name=gltB {ECO:0000313|EMBL:OFS76205.1};
GN ORFNames=HMPREF3173_04500 {ECO:0000313|EMBL:OFS76205.1};
OS Pseudomonas sp. HMSC08G10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1581141 {ECO:0000313|EMBL:OFS76205.1, ECO:0000313|Proteomes:UP000179079};
RN [1] {ECO:0000313|EMBL:OFS76205.1, ECO:0000313|Proteomes:UP000179079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08G10 {ECO:0000313|EMBL:OFS76205.1,
RC ECO:0000313|Proteomes:UP000179079};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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:OFS76205.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWMZ01000018; OFS76205.1; -; Genomic_DNA.
DR RefSeq; WP_043208577.1; NZ_KV793294.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000179079; 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 1481 AA; 161889 MW; ACB85DA59ED73E2A CRC64;
MKTGLYHPEE FKDNCGFGLI AHMTGEASHH LLQTAMQALT CMTHRGGINA DGKTGDGCGL
LMQKPDQFLR AVAQEHFAVE LPKQYAVGMV FFNQDPVKAE AARANMDREI INAGLKLVGW
RKVPIDTSVL GRLALERLPQ IEQVFIGGEG LSDQEFAIKL FSARRRSSVA NAHDADHYIC
SFSHKTIIYK GLMMPADLSA FYPDLGDERL KTAICVFHQR FSTNTLPKWP LAQPFRFLAH
NGEINTITGN RNWAIARRTK FANDLIPDLE ELGPLVNRVG SDSSSMDNML ELMVTGGIDL
FRGVRMLVPP AWQNVETMDA DLRAFYEYNS MHMEPWDGPA GIVMTEGRHA VCLLDRNGLR
PARWVTTKNG YITLASEIGV WDYKPEDVLA KGRVGPGQIF AVDTETGQIL DTDAIDNRLK
SRHPYKRWLR QHALRIQATL TDDQGVASYD ADQLKQYMKM FQVTFEERDQ VLRPLGEQGQ
EAVGSMGDDT PMAVLSQRVR SPYDFFRQQF AQVTNPPIDP LREAIVMSLE ICLGAERNIF
QESPEHASRV ILSSPVISPA KWRSLMNLER EGFDRQLIDL NYEESVGLEA AIRNIADQAE
EAVRSGKTQL VLSDRYIAPG KLPVHASLAV GAVHHRLTEQ GLRCDSNILV ETATARDPHH
FAVLLGFGAS AVYPYLSYEV LADLIRTGEV LGDLDEVFKY YRKGISKGLL KILSKMGIST
IASYRGAQLF EAVGLAEEVV GLSFKGVASR IKGARFVDLE NDQKLLAAEA WSARKPIQQG
GLLKFVHGGE YHAYNPDVVN TLQAAVQKGD YAKFKEYTTL VDQRPVSMIR DLLKVKLAEQ
PLALDQVEPL EDILKRFDSA GISLGALSPE AHEALAEAMN RLGARSNSGE GGEDPARYGT
IKSSKIKQVA TGRFGVTPEY LVNAEVLQIK VAQGAKPGEG GQLPGGKVNG LIARLRYAVP
GVTLISPPPH HDIYSIEDLA QLIYDLKQVN PQALVSVKLV AEAGVGTIAA GVAKAYADLI
TISGYDGGTG ASPLTSIKYA GAPWELGLAE THQTLRGNDL RGKVRVQTDG GLKTGLDVIK
AAILGAESFG FGTAPMIALG CKYLRICHLN NCATGVATQN DKLRKDHYIG TVDMVVNFFT
FVAEETREWL AKLGVRSLGE LIGRTDLLDI LPGDTERQQY LDLSPLLGSS HIPADKPQFC
EVDKNPPFDK GELAEKMVEM ALPAIRDLSG GEFSLDICNC DRSIGARISG EIARLHGNQG
MAGAPITFRF KGTAGQSFGV WNAGGLNLHL EGDANDYVGK GMTGGKLTIV PPAGSPFETQ
HSAIVGNTCL YGATGGKLFA AGTAGERFAV RNSGAHAVVE GTGDHCCEYM TGGFVCVLGK
TGYNFGSGMT GGFAYVLDMD NTFVDKLNHE LVEIQRISGE AMEAYRSHLA RVLGEYVEET
GSEWGRELSE NLDDYVRRFW LVKPKAANLK QLLSSTRANP Q
//
