GLTD_ECOLI
ID GLTD_ECOLI Reviewed; 472 AA.
AC P09832; Q2M8Z9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Glutamate synthase [NADPH] small chain;
DE EC=1.4.1.13 {ECO:0000269|PubMed:4565085};
DE AltName: Full=Glutamate synthase subunit beta;
DE Short=GLTS beta chain;
DE AltName: Full=NADPH-GOGAT;
GN Name=gltD; Synonyms=aspB; OrderedLocusNames=b3213, JW3180;
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 PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND 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 [7]
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).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711};
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 P09832; P09831: gltB; NbExp=3; IntAct=EBI-544293, EBI-551179;
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.
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DR EMBL; M18747; AAA23905.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58015.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76245.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77257.1; -; Genomic_DNA.
DR PIR; G65112; G65112.
DR RefSeq; NP_417680.1; NC_000913.3.
DR RefSeq; WP_000081674.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P09832; -.
DR SMR; P09832; -.
DR BioGRID; 4262427; 198.
DR ComplexPortal; CPX-5041; Glutamate synthase [NADPH] complex.
DR DIP; DIP-9803N; -.
DR IntAct; P09832; 6.
DR STRING; 511145.b3213; -.
DR SWISS-2DPAGE; P09832; -.
DR jPOST; P09832; -.
DR PaxDb; P09832; -.
DR PRIDE; P09832; -.
DR EnsemblBacteria; AAC76245; AAC76245; b3213.
DR EnsemblBacteria; BAE77257; BAE77257; BAE77257.
DR GeneID; 66672885; -.
DR GeneID; 947723; -.
DR KEGG; ecj:JW3180; -.
DR KEGG; eco:b3213; -.
DR PATRIC; fig|511145.12.peg.3308; -.
DR EchoBASE; EB0399; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_3_6; -.
DR InParanoid; P09832; -.
DR OMA; IDYGRCS; -.
DR PhylomeDB; P09832; -.
DR BioCyc; EcoCyc:GLUSYNSMALL-MON; -.
DR BioCyc; MetaCyc:GLUSYNSMALL-MON; -.
DR BRENDA; 1.4.1.13; 2026.
DR SABIO-RK; P09832; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00689.
DR PRO; PR:P09832; -.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR006006; GltD-like.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR42783:SF1; PTHR42783:SF1; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR TIGRFAMs; TIGR01318; gltD_gamma_fam; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Direct protein sequencing;
KW Glutamate biosynthesis; Iron; Iron-sulfur; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841"
FT CHAIN 2..472
FT /note="Glutamate synthase [NADPH] small chain"
FT /id="PRO_0000170800"
FT DOMAIN 38..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT CONFLICT 38..51
FT /note="GQAKAQADRCLSCG -> ARPKRRLTAACRAA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="E -> K (in Ref. 1; AAA23905)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="V -> C (in Ref. 1; AAA23905)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..270
FT /note="VYAALPFLIANTKQ -> CTQRCRSSSPTPNS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..313
FT /note="KH -> ND (in Ref. 1; AAA23905)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..400
FT /note="GRRRAEIVAGSEHIVPADAVIMAFG -> ASPRGDRCRFRTYRTGRCGDHGV
FT W (in Ref. 1; AAA23905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52015 MW; F188CE1086040433 CRC64;
MSQNVYQFID LQRVDPPKKP LKIRKIEFVE IYEPFSEGQA KAQADRCLSC GNPYCEWKCP
VHNYIPNWLK LANEGRIFEA AELSHQTNTL PEVCGRVCPQ DRLCEGSCTL NDEFGAVTIG
NIERYINDKA FEMGWRPDMS GVKQTGKKVA IIGAGPAGLA CADVLTRNGV KAVVFDRHPE
IGGLLTFGIP AFKLEKEVMT RRREIFTGMG IEFKLNTEVG RDVQLDDLLS DYDAVFLGVG
TYQSMRGGLE NEDADGVYAA LPFLIANTKQ LMGFGETRDE PFVSMEGKRV VVLGGGDTAM
DCVRTSVRQG AKHVTCAYRR DEENMPGSRR EVKNAREEGV EFKFNVQPLG IEVNGNGKVS
GVKMVRTEMG EPDAKGRRRA EIVAGSEHIV PADAVIMAFG FRPHNMEWLA KHSVELDSQG
RIIAPEGSDN AFQTSNPKIF AGGDIVRGSD LVVTAIAEGR KAADGIMNWL EV
