DCEA_ECOLI
ID DCEA_ECOLI Reviewed; 466 AA.
AC P69908; P80063; Q2M7H9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glutamate decarboxylase alpha;
DE Short=GAD-alpha;
DE EC=4.1.1.15;
GN Name=gadA; Synonyms=gadS; OrderedLocusNames=b3517, JW3485;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1522060; DOI=10.1128/jb.174.18.5820-5826.1992;
RA Smith D.K., Kassam T., Singh B., Elliott J.F.;
RT "Escherichia coli has two homologous glutamate decarboxylase genes that map
RT to distinct loci.";
RL J. Bacteriol. 174:5820-5826(1992).
RN [2]
RP PROTEIN SEQUENCE, AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-466.
RC STRAIN=ATCC 11246;
RX PubMed=1740158; DOI=10.1111/j.1432-1033.1992.tb16609.x;
RA Maras B., Sweeney G., Barra D., Bossa F., John R.A.;
RT "The amino acid sequence of glutamate decarboxylase from Escherichia coli.
RT Evolutionary relationship between mammalian and bacterial enzymes.";
RL Eur. J. Biochem. 204:93-98(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 1-22.
RX PubMed=7764225; DOI=10.1271/bbb.57.1568;
RA Yoshida T., Yamashino T., Ueguchi C., Mizuno T.;
RT "Expression of the Escherichia coli dimorphic glutamic acid decarboxylases
RT is regulated by the nucleoid protein H-NS.";
RL Biosci. Biotechnol. Biochem. 57:1568-1569(1993).
RN [7]
RP PROTEIN SEQUENCE OF 382-392.
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 [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).
RN [9]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 11246;
RX PubMed=10383761; DOI=10.1046/j.1365-2958.1999.01430.x;
RA De Biase D., Tramonti A., Bossa F., Visca P.;
RT "The response to stationary-phase stress conditions in Escherichia coli:
RT role and regulation of the glutamic acid decarboxylase system.";
RL Mol. Microbiol. 32:1198-1211(1999).
RN [10]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 11246;
RX PubMed=11976288; DOI=10.1128/jb.184.10.2603-2613.2002;
RA Tramonti A., Visca P., De Canio M., Falconi M., De Biase D.;
RT "Functional characterization and regulation of gadX, a gene encoding an
RT AraC/XylS-like transcriptional activator of the Escherichia coli glutamic
RT acid decarboxylase system.";
RL J. Bacteriol. 184:2603-2613(2002).
RN [11]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12399493; DOI=10.1128/jb.184.22.6225-6234.2002;
RA Masuda N., Church G.M.;
RT "Escherichia coli gene expression responsive to levels of the response
RT regulator EvgA.";
RL J. Bacteriol. 184:6225-6234(2002).
RN [12]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12;
RX PubMed=12446650; DOI=10.1128/jb.184.24.7001-7012.2002;
RA Ma Z., Richard H., Tucker D.L., Conway T., Foster J.W.;
RT "Collaborative regulation of Escherichia coli glutamate-dependent acid
RT resistance by two AraC-like regulators, GadX and GadW (YhiW).";
RL J. Bacteriol. 184:7001-7012(2002).
RN [13]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=12867478; DOI=10.1128/jb.185.15.4644-4647.2003;
RA Waterman S.R., Small P.L.C.;
RT "Transcriptional expression of Escherichia coli glutamate-dependent acid
RT resistance genes gadA and gadBC in an hns rpoS mutant.";
RL J. Bacteriol. 185:4644-4647(2003).
RN [14]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12694615; DOI=10.1046/j.1365-2958.2003.03477.x;
RA Masuda N., Church G.M.;
RT "Regulatory network of acid resistance genes in Escherichia coli.";
RL Mol. Microbiol. 48:699-712(2003).
RN [15]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12;
RX PubMed=12940989; DOI=10.1046/j.1365-2958.2003.03633.x;
RA Ma Z., Gong S., Richard H., Tucker D.L., Conway T., Foster J.W.;
RT "GadE (YhiE) activates glutamate decarboxylase-dependent acid resistance in
RT Escherichia coli K-12.";
RL Mol. Microbiol. 49:1309-1320(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RA Dutyshev D.I., Darii E.L., Fomenkova N.P., Pechik I.V., Polyakov K.M.,
RA Nikonov S.V., Andreeva N.S., Sukhareva B.S.;
RT "Structure of the complex of Escherichia coli glutamate decarboxylase
RT (gadA) with glutarate at 2.05 A resolution.";
RL Submitted (SEP-2004) to the PDB data bank.
CC -!- FUNCTION: Converts glutamate to gamma-aminobutyrate (GABA), consuming
CC one intracellular proton in the reaction. The gad system helps to
CC maintain a near-neutral intracellular pH when cells are exposed to
CC extremely acidic conditions. The ability to survive transit through the
CC acidic conditions of the stomach is essential for successful
CC colonization of the mammalian host by commensal and pathogenic
CC bacteria.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homohexamer.
CC -!- INDUCTION: By acidic conditions. Expression is regulated by a complex
CC system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW and GadX. The
CC level of involvement for each regulator varies depending upon the
CC growth phase and the medium. {ECO:0000269|PubMed:10383761,
CC ECO:0000269|PubMed:11976288, ECO:0000269|PubMed:12399493,
CC ECO:0000269|PubMed:12446650, ECO:0000269|PubMed:12694615,
CC ECO:0000269|PubMed:12867478, ECO:0000269|PubMed:12940989}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/GLDP/";
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DR EMBL; M84024; AAA23833.1; -; Genomic_DNA.
DR EMBL; X63123; CAA44834.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18493.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76542.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77777.1; -; Genomic_DNA.
DR PIR; S47737; S24234.
DR RefSeq; NP_417974.1; NC_000913.3.
DR RefSeq; WP_000372240.1; NZ_SSYX01000029.1.
DR PDB; 1XEY; X-ray; 2.05 A; A/B=1-466.
DR PDBsum; 1XEY; -.
DR AlphaFoldDB; P69908; -.
DR SASBDB; P69908; -.
DR SMR; P69908; -.
DR BioGRID; 4261597; 2.
DR DIP; DIP-36201N; -.
DR IntAct; P69908; 15.
DR MINT; P69908; -.
DR STRING; 511145.b3517; -.
DR DrugBank; DB03553; Glutaric Acid.
DR jPOST; P69908; -.
DR PaxDb; P69908; -.
DR PRIDE; P69908; -.
DR EnsemblBacteria; AAC76542; AAC76542; b3517.
DR EnsemblBacteria; BAE77777; BAE77777; BAE77777.
DR GeneID; 66672598; -.
DR GeneID; 948027; -.
DR KEGG; ecj:JW3485; -.
DR KEGG; eco:b3517; -.
DR PATRIC; fig|511145.12.peg.3626; -.
DR EchoBASE; EB4302; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_019582_0_0_6; -.
DR InParanoid; P69908; -.
DR OMA; IIWRDES; -.
DR PhylomeDB; P69908; -.
DR BioCyc; EcoCyc:GLUTDECARBOXA-MON; -.
DR BioCyc; MetaCyc:GLUTDECARBOXA-MON; -.
DR BRENDA; 4.1.1.15; 2026.
DR EvolutionaryTrace; P69908; -.
DR PRO; PR:P69908; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR GO; GO:0051454; P:intracellular pH elevation; IMP:EcoCyc.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR010107; Glutamate_decarboxylase.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR43321; PTHR43321; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..466
FT /note="Glutamate decarboxylase alpha"
FT /id="PRO_0000146978"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..127
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 64
FT /note="C -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="H -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="C -> S (in Ref. 2; CAA44834)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="T -> N (in Ref. 2; CAA44834)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="L -> V (in Ref. 2; CAA44834)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:1XEY"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:1XEY"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1XEY"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 126..147
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1XEY"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:1XEY"
FT TURN 274..278
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 322..357
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:1XEY"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:1XEY"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:1XEY"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:1XEY"
FT HELIX 431..449
FT /evidence="ECO:0007829|PDB:1XEY"
SQ SEQUENCE 466 AA; 52685 MW; 86F963E710553E22 CRC64;
MDQKLLTDFR SELLDSRFGA KAISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL
ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC VNMVADLWHA PAPKNGQAVG
TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK PTDKPNLVCG PVQICWHKFA RYWDVELREI
PMRPGQLFMD PKRMIEACDE NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM
HIDAASGGFL APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV
FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA AYLADEIAKL
GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR LRGWQVPAFT LGGEATDIVV
MRIMCRRGFE MDFAELLLED YKASLKYLSD HPKLQGIAQQ NSFKHT
