ID A0A1V4LLH0_9PSED Unreviewed; 1481 AA.
AC A0A1V4LLH0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:OPK08108.1};
GN ORFNames=BZ163_23800 {ECO:0000313|EMBL:OPK08108.1};
OS Pseudomonas sp. VI4.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1941346 {ECO:0000313|EMBL:OPK08108.1, ECO:0000313|Proteomes:UP000189889};
RN [1] {ECO:0000313|EMBL:OPK08108.1, ECO:0000313|Proteomes:UP000189889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VI4.1 {ECO:0000313|EMBL:OPK08108.1,
RC ECO:0000313|Proteomes:UP000189889};
RA Imperato V., Thijs S., Mcammond B., Douwen Y., Broeders P., Kowalkowski L.,
RA Gawronski S., Vangronsveld J.;
RT "Draft genome sequence of Pseudomonas yorbenii VI4.1, a hydrocarbonoclastic
RT isolate from crude oil contaminated soil in Bobrka, Poland.";
RL Submitted (FEB-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:OPK08108.1}.
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; MULM01000173; OPK08108.1; -; Genomic_DNA.
DR Proteomes; UP000189889; 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..404
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1481 AA; 162216 MW; C6AF0C0A24876333 CRC64;
MKAGLYQPDE FKDNCGFGLI AHMQGEPSHT LLQTAVEALT CMTHRGGINA DGKTGDGCGL
LIQKPDAFLR AIAQETFGVE LPKQYAVGMV FFNQDPVKAE AARENMNREL LAEGLQLVGW
RKVPIDTSVL GRLALERLPQ IEQVYIGGEG LSDQDMAIKL FSARRRSSVA NAADVDHYIC
SFSHKTIIYK GLMMPADLTA FYPDLSDQRL QTSICVFHQR FSTNTLPKWP LAQPFRFLAH
NGEINTITGN RNWAQARRTK FTNDLMDLEE LGPLVNRVGS DSSSMDNMLE LMVTGGIDLF
RGVRMIIPPA WQNVETMDPD LRAFYEYNSM HMEPWDGPAG VVMTDGRYAV CLLDRNGLRP
ARWVTTKNGF ITLASEIGVW NYQPEDVIAK GRVGPGQIFA VDTETGQILD TDAIDNRLKS
RHPYKQWLRK NALRIQATME DNDHGSAFYD VDQLKQYMKM YQVTFEERDQ VLRPLGEQGY
EAVGSMGDDT PMAVLSQRVR TPYDYFRQQF AQVTNPPIDP LREAIVMSLE ICLGAERNIF
QESPEHASRV ILSSPVISPA KWRSLMNLDR PGFERAIIDL NYDESVGLEA AVRNVADQAE
EAVRAGRTQI VLSDRHIAPG KLPIHASLAT GAVHHRLTEK GLRCDSNILV ETATARDPHH
FAVLIGFGAS AVYPFLAYEV LGDLIRTGEV LGDLYEVFKN YRKGITKGLL KILSKMGIST
IASYRGAQLF EAIGLSEEVC DLSFRGVPSR IKGARFVDIE AEQKALAAEA WSPRKPIQQG
GLLKFVHGGE YHAYNPDVVN TLQAAVQQGD YGKFKEYTAL VDNRPVSMIR DLFKVKTLDT
PLDISEIEPL ESVLKRFDSA GISLGALSPE AHEALAEAMN RLGARSNSGE GGEDPARYGT
IKSSKIKQVA TGRFGVTPEY LVNAEVLQIK VAQGAKPGEG GQLPGGKVNG LIAKLRYAVP
GVTLISPPPH HDIYSIEDLS QLIFDLKQVN PKALVSVKLV AEAGVGTIAA GVAKAYADLI
TISGYDGGTG ASPLTSIKYA GAPWELGLAE THQTLRGNDL RGKVRVQTDG GLKTGLDVIK
AAILGAESFG FGTAPMIALG CKYLRICHLN NCATGVATQN EKLRKDHYIG TVDMVVNFFT
YVAEETREWL AKLGVRSLEE LIGRTDLLDI LEGQTAKQNH LDLTPLLGSD HIPADKPQFC
QVERNPPFDK GLLAEKMVDL ATSAINDMSG ANFALDICNC DRSIGARISG EIARKYGNQG
MASAPITFRF NGTAGQSFGV WNAGGLNMYL EGDANDYVGK GMTGGKLVIV PPKGSVYKTQ
DSAIIGNTCL YGATGGKLFA AGTAGERFAV RNSGAHTVVE GTGDHCCEYM TGGFVCVLGK
TGYNFGSGMT GGFAYVLDQD NSFVDRVNHE LVEIQRISGE AMEAYRSHLQ RVLNEYVEET
DSEWGRNLAE NLDDYLRRFW LVKPKAANLK SLLSSTRANP Q
//
