GLTB_ECOLI
ID GLTB_ECOLI Reviewed; 1486 AA.
AC P09831; Q2M900;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Glutamate synthase [NADPH] large chain;
DE EC=1.4.1.13 {ECO:0000269|PubMed:4565085};
DE AltName: Full=Glutamate synthase subunit alpha;
DE Short=GLTS alpha chain;
DE AltName: Full=NADPH-GOGAT;
DE Flags: Precursor;
GN Name=gltB; Synonyms=aspB; OrderedLocusNames=b3212, JW3179;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=3326786; DOI=10.1016/0378-1119(87)90207-1;
RA Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L.M., Flores N.,
RA Becerril B., Valle F., Bolivar F.;
RT "Determination of the nucleotide sequence for the glutamate synthase
RT structural genes of Escherichia coli K-12.";
RL Gene 60:1-11(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.
RX PubMed=1673677; DOI=10.1128/jb.173.10.3261-3264.1991;
RA Velazquez L., Camarena L., Reyes J.L., Bastarrachea F.;
RT "Mutations affecting the Shine-Dalgarno sequences of the untranslated
RT region of the Escherichia coli gltBDF operon.";
RL J. Bacteriol. 173:3261-3264(1991).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=W;
RX PubMed=4565085; DOI=10.1016/s0021-9258(19)44642-5;
RA Miller R.E., Stadtman E.R.;
RT "Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein.";
RL J. Biol. Chem. 247:7407-7419(1972).
RN [6]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2643092;
RA Gosset G., Merino E., Recillas F., Oliver G., Becerril B., Bolivar F.;
RT "Amino acid sequence analysis of the glutamate synthase enzyme from
RT Escherichia coli K-12.";
RL Protein Seq. Data Anal. 2:9-16(1989).
CC -!- FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate
CC into two molecules of L-glutamate. {ECO:0000269|PubMed:4565085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000269|PubMed:4565085};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:4565085};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:4565085};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.3 uM for 2-oxoglutarate {ECO:0000269|PubMed:4565085};
CC KM=250 uM for L-glutamine {ECO:0000269|PubMed:4565085};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:4565085};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC route): step 1/1.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC -!- SUBUNIT: Aggregate of 4 catalytic active heterodimers, consisting of a
CC large and a small subunit. {ECO:0000269|PubMed:4565085}.
CC -!- INTERACTION:
CC P09831; P09832: gltD; NbExp=3; IntAct=EBI-551179, EBI-544293;
CC -!- MISCELLANEOUS: Glutamine binds to the large subunit and transfers the
CC amido group to 2-oxoglutarate that apparently binds to the small
CC subunit.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23904.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA23906.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA58014.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77256.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; M18747; AAA23904.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA58014.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76244.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77256.1; ALT_INIT; Genomic_DNA.
DR EMBL; M68876; AAA23906.1; ALT_INIT; Genomic_DNA.
DR PIR; F65112; F65112.
DR RefSeq; NP_417679.2; NC_000913.3.
DR RefSeq; WP_001300352.1; NZ_LN832404.1.
DR AlphaFoldDB; P09831; -.
DR SMR; P09831; -.
DR BioGRID; 4263210; 352.
DR ComplexPortal; CPX-5041; Glutamate synthase [NADPH] complex.
DR DIP; DIP-9802N; -.
DR IntAct; P09831; 8.
DR STRING; 511145.b3212; -.
DR MEROPS; C44.003; -.
DR jPOST; P09831; -.
DR PaxDb; P09831; -.
DR PRIDE; P09831; -.
DR EnsemblBacteria; AAC76244; AAC76244; b3212.
DR EnsemblBacteria; BAE77256; BAE77256; BAE77256.
DR GeneID; 947724; -.
DR KEGG; ecj:JW3179; -.
DR KEGG; eco:b3212; -.
DR PATRIC; fig|511145.12.peg.3307; -.
DR EchoBASE; EB0398; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_6; -.
DR InParanoid; P09831; -.
DR OMA; TVFRLQH; -.
DR PhylomeDB; P09831; -.
DR BioCyc; EcoCyc:GLUSYNLARGE-MON; -.
DR BioCyc; MetaCyc:GLUSYNLARGE-MON; -.
DR BRENDA; 1.4.1.13; 2026.
DR SABIO-RK; P09831; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00689.
DR PRO; PR:P09831; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009342; C:glutamate synthase complex (NADPH); IPI:ComplexPortal.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IDA:EcoCyc.
DR GO; GO:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019676; P:ammonia assimilation cycle; IDA:ComplexPortal.
DR GO; GO:0006537; P:glutamate biosynthetic process; IDA:EcoCyc.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IDA:ComplexPortal.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.60.20.10; -; 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 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; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Amino-acid biosynthesis; Direct protein sequencing; FAD;
KW Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase;
KW Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW Zymogen.
FT PROPEP 1..11
FT /id="PRO_0000011620"
FT CHAIN 12..1486
FT /note="Glutamate synthase [NADPH] large chain"
FT /id="PRO_0000011621"
FT DOMAIN 12..402
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 1049..1101
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1102
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1108
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1113
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT CONFLICT 74..78
FT /note="GWRLA -> LAFR (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="E -> N (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..209
FT /note="LCMPTDLPRFYLDLADLRLES -> CVCRRICRVLSGSCGPASGM (in
FT Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..251
FT /note="LAQPFRYLAHNGEINTITGNRQWA -> WRNRSAIWRITVKSTPSPVTANG
FT (in Ref. 1; AAA23904 and 4; AAA23906)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="N -> K (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="A -> T (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="D -> H (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 1255..1259
FT /note="THGDQ -> DARRS (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 1342
FT /note="G -> A (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
FT CONFLICT 1345
FT /note="G -> R (in Ref. 1; AAA23904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1486 AA; 163297 MW; 19C1E5B04F94A33D CRC64;
MLYDKSLERD NCGFGLIAHI EGEPSHKVVR TAIHALARMQ HRGAILADGK TGDGCGLLLQ
KPDRFFRIVA QERGWRLAKN YAVGMLFLNK DPELAAAARR IVEEELQRET LSIVGWRDVP
TNEGVLGEIA LSSLPRIEQI FVNAPAGWRP RDMERRLFIA RRRIEKRLEA DKDFYVCSLS
NLVNIYKGLC MPTDLPRFYL DLADLRLESA ICLFHQRFST NTVPRWPLAQ PFRYLAHNGE
INTITGNRQW ARARTYKFQT PLIPDLHDAA PFVNETGSDS SSMDNMLELL LAGGMDIIRA
MRLLVPPAWQ NNPDMDPELR AFFDFNSMHM EPWDGPAGIV MSDGRFAACN LDRNGLRPAR
YVITKDKLIT CASEVGIWDY QPDEVVEKGR VGPGELMVID TRSGRILHSA ETDDDLKSRH
PYKEWMEKNV RRLVPFEDLP DEEVGSRELD DDTLASYQKQ FNYSAEELDS VIRVLGENGQ
EAVGSMGDDT PFAVLSSQPR IIYDYFRQQF AQVTNPPIDP LREAHVMSLA TSIGREMNVF
CEAEGQAHRL SFKSPILLYS DFKQLTTMKE EHYRADTLDI TFDVTKTTLE ATVKELCDKA
EKMVRSGTVL LVLSDRNIAK DRLPVPAPMA VGAIQTRLVD QSLRCDANII VETASARDPH
HFAVLLGFGA TAIYPYLAYE TLGRLVDTHA IAKDYRTVML NYRNGINKGL YKIMSKMGIS
TIASYRCSKL FEAVGLHDDV VGLCFQGAVS RIGGASFEDF QQDLLNLSKR AWLARKPISQ
GGLLKYVHGG EYHAYNPDVV RTLQQAVQSG EYSDYQEYAK LVNERPATTL RDLLAITPGE
NAVNIADVEP ASELFKRFDT AAMSIGALSP EAHEALAEAM NSIGGNSNSG EGGEDPARYG
TNKVSRIKQV ASGRFGVTPA YLVNADVIQI KVAQGAKPGE GGQLPGDKVT PYIAKLRYSV
PGVTLISPPP HHDIYSIEDL AQLIFDLKQV NPKAMISVKL VSEPGVGTIA TGVAKAYADL
ITIAGYDGGT GASPLSSVKY AGCPWELGLV ETQQALVANG LRHKIRLQVD GGLKTGVDII
KAAILGAESF GFGTGPMVAL GCKYLRICHL NNCATGVATQ DDKLRKNHYH GLPFKVTNYF
EFIARETREL MAQLGVTRLV DLIGRTDLLK ELDGFTAKQQ KLALSKLLET AEPHPGKALY
CTENNPPFDN GLLNAQLLQQ AKPFVDERQS KTFWFDIRNT DRSVGASLSG YIAQTHGDQG
LAADPIKAYF NGTAGQSFGV WNAGGVELYL TGDANDYVGK GMAGGLIAIR PPVGSAFRSH
EASIIGNTCL YGATGGRLYA AGRAGERFGV RNSGAITVVE GIGDNGCEYM TGGIVCILGK
TGVNFGAGMT GGFAYVLDES GDFRKRVNPE LVEVLSVDAL AIHEEHLRGL ITEHVQHTGS
QRGEEILANW STFATKFALV KPKSSDVKAL LGHRSRSAAE LRVQAQ
