ELBB_ECOLI
ID ELBB_ECOLI Reviewed; 217 AA.
AC P0ABU5; P26428; P76673; Q2M903;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glyoxalase ElbB {ECO:0000303|PubMed:26678554};
DE EC=4.2.1.- {ECO:0000269|PubMed:26678554};
DE AltName: Full=Sigma cross-reacting protein 27A {ECO:0000303|PubMed:1575737};
DE Short=SCRP-27A {ECO:0000303|PubMed:1575737};
GN Name=elbB {ECO:0000303|PubMed:26678554};
GN Synonyms=elb2 {ECO:0000303|PubMed:9603997}, yzzB;
GN OrderedLocusNames=b3209, JW3176;
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 / W3110 / ATCC 27325 / DSM 5911;
RA Smillie D.A., Fujita N., Townsley F.M., Ishihama A., Hayward R.S.;
RT "Sequence and characterisation of the gene encoding the sigma cross-
RT reacting protein 27A in Escherichia coli.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
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 1-24.
RX PubMed=1575737; DOI=10.1016/0006-291x(92)90636-y;
RA Ueshima R., Fujita N., Ishihama A.;
RT "Identification of Escherichia coli proteins cross-reacting with antibodies
RT against region 2.2 peptide of RNA polymerase sigma subunit.";
RL Biochem. Biophys. Res. Commun. 184:634-639(1992).
RN [5]
RP POSSIBLE FUNCTION.
RX PubMed=9603997; DOI=10.1093/oxfordjournals.jbchem.a022047;
RA Hemmi H., Ohnuma S., Nagaoka K., Nishino T.;
RT "Identification of genes affecting lycopene formation in Escherichia coli
RT transformed with carotenoid biosynthetic genes: candidates for early genes
RT in isoprenoid biosynthesis.";
RL J. Biochem. 123:1088-1096(1998).
RN [6]
RP FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=26678554; DOI=10.1093/femsle/fnv239;
RA Lee C., Lee J., Lee J.Y., Park C.;
RT "Characterization of the Escherichia coli YajL, YhbO and ElbB
RT glyoxalases.";
RL FEMS Microbiol. Lett. 363:0-0(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS), AND SUBUNIT.
RG Northeast structural genomics consortium (NESG);
RA Benach J., Edstrom W., Ma L.C., Xiao R., Acton T.B., Rost B.,
RA Montelione G.T., Hunt J.F.;
RT "X-Ray structure Of ElbB from E. Coli. Northeast Structural Genomics
RT Research Consortium (Nesg) Target Er105.";
RL Submitted (APR-2003) to the PDB data bank.
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Displays glyoxalase activity, catalyzing the conversion of
CC glyoxal to glycolate (PubMed:26678554). However, this apparent
CC glyoxalase activity may reflect a protein deglycase activity, which
CC could be the primary function of this protein like other DJ-1
CC superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is
CC not able to use methylglyoxal as substrate (PubMed:26678554).
CC {ECO:0000269|PubMed:26678554, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxal + H2O = glycolate + H(+); Xref=Rhea:RHEA:51672,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:34779; Evidence={ECO:0000269|PubMed:26678554};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.21 mM for glyoxal (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:26678554};
CC Note=kcat is 0.48 min(-1) with glyoxal as substrate (at pH 7.4 and 37
CC degrees Celsius). {ECO:0000269|PubMed:26678554};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:16021622, ECO:0000305|Ref.7}.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought (PubMed:9603997) to be involved in the
CC early steps of isoprenoid biosynthesis. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58011.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D13188; BAA02487.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58011.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76241.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77253.1; -; Genomic_DNA.
DR PIR; C65112; C65112.
DR RefSeq; NP_417676.2; NC_000913.3.
DR RefSeq; WP_001300411.1; NZ_SSZK01000007.1.
DR PDB; 1OY1; X-ray; 2.95 A; A/B/C/D=1-217.
DR PDB; 1VHQ; X-ray; 1.65 A; A/B=1-217.
DR PDBsum; 1OY1; -.
DR PDBsum; 1VHQ; -.
DR AlphaFoldDB; P0ABU5; -.
DR SMR; P0ABU5; -.
DR BioGRID; 4262428; 13.
DR BioGRID; 852212; 5.
DR DIP; DIP-48002N; -.
DR IntAct; P0ABU5; 6.
DR STRING; 511145.b3209; -.
DR MEROPS; C56.975; -.
DR SWISS-2DPAGE; P0ABU5; -.
DR jPOST; P0ABU5; -.
DR PaxDb; P0ABU5; -.
DR PRIDE; P0ABU5; -.
DR EnsemblBacteria; AAC76241; AAC76241; b3209.
DR EnsemblBacteria; BAE77253; BAE77253; BAE77253.
DR GeneID; 58388186; -.
DR GeneID; 947903; -.
DR KEGG; ecj:JW3176; -.
DR KEGG; eco:b3209; -.
DR PATRIC; fig|1411691.4.peg.3522; -.
DR EchoBASE; EB1356; -.
DR eggNOG; COG3155; Bacteria.
DR HOGENOM; CLU_072952_1_0_6; -.
DR InParanoid; P0ABU5; -.
DR OMA; AQVQCFA; -.
DR PhylomeDB; P0ABU5; -.
DR BioCyc; EcoCyc:EG11383-MON; -.
DR BioCyc; MetaCyc:EG11383-MON; -.
DR EvolutionaryTrace; P0ABU5; -.
DR PRO; PR:P0ABU5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0045828; P:positive regulation of isoprenoid metabolic process; IMP:EcoliWiki.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR026041; ElbB.
DR PANTHER; PTHR10224:SF12; PTHR10224:SF12; 1.
DR PIRSF; PIRSF006320; Elb2; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Reference proteome.
FT CHAIN 1..217
FT /note="Glyoxalase ElbB"
FT /id="PRO_0000201681"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P31658"
FT CONFLICT 111
FT /note="C -> S (in Ref. 1; BAA02487)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..217
FT /note="AQNIAEAASGIDKLVSRVLVLAE -> RRTLQKRRAALISWFPACWFWLNE
FT (in Ref. 1; BAA02487)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1VHQ"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1VHQ"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:1VHQ"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1VHQ"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1VHQ"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:1VHQ"
FT TURN 68..73
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1VHQ"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:1VHQ"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1VHQ"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1VHQ"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:1VHQ"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1VHQ"
FT HELIX 198..216
FT /evidence="ECO:0007829|PDB:1VHQ"
SQ SEQUENCE 217 AA; 22982 MW; 48A7957C29384DAC CRC64;
MKKIGVILSG CGVYDGSEIH EAVLTLLAIS RSGAQAVCFA PDKQQVDVIN HLTGEAMTET
RNVLIEAARI TRGEIRPLAQ ADAAELDALI VPGGFGAAKN LSNFASLGSE CTVDRELKAL
AQAMHQAGKP LGFMCIAPAM LPKIFDFPLR LTIGTDIDTA EVLEEMGAEH VPCPVDDIVV
DEDNKIVTTP AYMLAQNIAE AASGIDKLVS RVLVLAE
