ID Q87V18_PSESM Unreviewed; 1481 AA.
AC Q87V18;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=Glutamate synthase, large subunit {ECO:0000313|EMBL:AAO58550.1};
GN Name=gltB {ECO:0000313|EMBL:AAO58550.1};
GN OrderedLocusNames=PSPTO_5123 {ECO:0000313|EMBL:AAO58550.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO58550.1, ECO:0000313|Proteomes:UP000002515};
RN [1] {ECO:0000313|EMBL:AAO58550.1, ECO:0000313|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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}.
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DR EMBL; AE016853; AAO58550.1; -; Genomic_DNA.
DR RefSeq; NP_794855.1; NC_004578.1.
DR RefSeq; WP_011105326.1; NC_004578.1.
DR STRING; 223283.PSPTO_5123; -.
DR MEROPS; C44.003; -.
DR GeneID; 1186808; -.
DR KEGG; pst:PSPTO_5123; -.
DR PATRIC; fig|223283.9.peg.5243; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_6; -.
DR OrthoDB; 9758182at2; -.
DR PhylomeDB; Q87V18; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; ISS:JCVI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; ISS:JCVI.
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:UP000002515}.
FT DOMAIN 15..404
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1481 AA; 162360 MW; CDABA86EBF700567 CRC64;
MKAGLYQPDE FKDNCGFGLI AHMQGEPSHH LLQTAVQALT CMTHRGGINA DGKTGDGCGL
LIQKPDGFLR AMASEHFGVE LPRQYAVGMV FLNQDDTKAK AARENMNREI LAEGLELVGW
RQVPIDTSVL GQLALERLPK IEQVYIGGEG LSDQEFAIKL FSARRRSSVA NAADSDHYIC
SFSHKTIIYK GLMMPADLTA FFPDLSDERL QTAICVFHQR FSTNTLPKWP LAQPFRFLAH
NGEINTITGN RNWAQARRTK FTNDLMDLDE LGPLVNRVGS DSSSMDNMLE LMVTGGIDLF
RGVRMIIPPA WQNVETMDPD LRAFYEYNSM HMEPWDGPAG IVMTEGRHAV CLLDRNGLRP
ARWVTTKNGY ITLASEIGVW DYKPEDVIAK GRVGPGQIFA VDTETGQILD TDAIDNRLKS
RHPYKQWLRK NALRIQATME DNDHGSAFYD SEQLKQYMKM YQVTFEERDQ VLRPLGEQGQ
EAVGSMGDDT PMAVLSRRVR SPYDYFRQQF AQVTNPPIDP LREAIVMSLE ICLGAERNIF
QESPEHASRV ILSSPVISPA KWRSLMNLER PGFERHIIDL NYDESLGLEA AVRNVADQAE
EAVRSGHTLI VLSDRHIAPG KLPVHASLAV GAVHHRLTEQ GLRCDSNILV ETATARDPHH
FAVLIGFGAS AVYPFLAYEV LGDLIRTGEV LGDLYEVFKN YRKGITKGLL KILSKMGIST
VASYRGAQLF EAIGLSEEVC NTSFRGVPSR LKGARFVDIE AEQKALAAEA WSPRKPIQQG
GLLKFVYGGE YHAYNPDVVS TLQAAVQQGD YSKFKEYTAL VDQRPVSMIR DLLQVKTLDQ
PLNIDEIEPL SEILKRFDSA GISLGALSPE AHEALAEAMN RLGARSNSGE GGEDPARYGT
IRSSKIKQIA TGRFGVTPEY LVNADVLQIK VAQGAKPGEG GQLPGGKVNG LIAKLRYAVP
GVTLISPPPH HDIYSIEDLS QLIFDLKQVN PAALVSVKLV AEAGVGTIAA GVAKAYADLI
TISGYDGGTG ASPLTSIKYA GAPWELGLAE THQTLRGNDL RGKVRVQTDG GLKTGLDVIK
AAILGAESFG FGTAPMIALG CKYLRICHLN NCATGVATQN EKLRKDHYIG TVDMVINFFT
YVAEETREWL ARLGVRTLEE LIGRTDLLDI LPGETEKQRH LDLTPLLGSD HIPADKPQFS
LVDRNPPFDK GLLAEKMVEL AKPAIEALSG GEFELDICNC DRSIGARISG EIARLHGNQG
MNKAPITFRF KGTAGQSFGV WNAGGLNMYL EGDANDYVGK GMTAGKLVIV PPKGSPFKTN
ESAIIGNTCL YGATGGKLFA AGTAGERFAV RNSGAHTVVE GTGDHCCEYM TGGFVCVLGK
TGYNFGSGMT GGFAYVLDQD NTFVDLVNHE LVEIQRISGE SMEAYRTHLQ SVLNEYVAET
DSEWGRNLAE NLDDYLRRFW LVKPKAANLK SLLSSTRANP Q
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