HCXB_ECO57
ID HCXB_ECO57 Reviewed; 361 AA.
AC P58409;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Hydroxycarboxylate dehydrogenase B {ECO:0000250|UniProtKB:P30178};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P30178};
DE AltName: Full=2-oxoglutarate reductase {ECO:0000250|UniProtKB:P30178};
DE AltName: Full=Hydroxyphenylpyruvate reductase {ECO:0000250|UniProtKB:P30178};
DE EC=1.1.1.237 {ECO:0000250|UniProtKB:P30178};
DE AltName: Full=Phenylpyruvate reductase {ECO:0000250|UniProtKB:P30178};
GN Name=hcxB {ECO:0000250|UniProtKB:P30178};
GN Synonyms=ybiC {ECO:0000312|EMBL:AAG55173.1};
GN OrderedLocusNames=Z1022, ECs0879;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate,
CC phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective
CC 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH
CC as a redox partner. Do not catalyze the reverse reactions.
CC {ECO:0000250|UniProtKB:P30178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyglutarate + NADP(+) = 2-oxoglutarate + H(+) + NADPH;
CC Xref=Rhea:RHEA:52308, ChEBI:CHEBI:11596, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH;
CC Xref=Rhea:RHEA:13449, ChEBI:CHEBI:11596, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenyllactate + NADP(+) = 3-phenylpyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:52692, ChEBI:CHEBI:8100, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenyllactate + NAD(+) = 3-phenylpyruvate + H(+) + NADH;
CC Xref=Rhea:RHEA:52688, ChEBI:CHEBI:8100, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-
CC hydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:10780,
CC ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.237;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NADP(+) = 3-(4-
CC hydroxyphenyl)pyruvate + H(+) + NADPH; Xref=Rhea:RHEA:10776,
CC ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.237;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-(3,4-dihydroxyphenyl)lactate + NADP(+) = 3-(3,4-
CC dihydroxyphenyl)pyruvate + H(+) + NADPH; Xref=Rhea:RHEA:57704,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29055, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:71492; EC=1.1.1.237;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-(3,4-dihydroxyphenyl)lactate + NAD(+) = 3-(3,4-
CC dihydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:57408,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29055, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:71492; EC=1.1.1.237;
CC Evidence={ECO:0000250|UniProtKB:P30178};
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG55173.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34302.1; -; Genomic_DNA.
DR PIR; A85589; A85589.
DR PIR; G90738; G90738.
DR RefSeq; NP_308906.1; NC_002695.1.
DR RefSeq; WP_000443495.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58409; -.
DR SMR; P58409; -.
DR STRING; 155864.EDL933_0924; -.
DR EnsemblBacteria; AAG55173; AAG55173; Z1022.
DR EnsemblBacteria; BAB34302; BAB34302; ECs_0879.
DR GeneID; 917618; -.
DR KEGG; ece:Z1022; -.
DR KEGG; ecs:ECs_0879; -.
DR PATRIC; fig|386585.9.peg.993; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_1_0_6; -.
DR OMA; HDIGMAS; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0047029; F:(R)-4-hydroxyphenyllactate dehydrogenase (NADPH) activity; IEA:RHEA.
DR GO; GO:0047995; F:hydroxyphenylpyruvate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102742; F:R(+)-3,4-dihydroxyphenyllactate:NADP+ oxidoreductase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1530.10; -; 2.
DR Gene3D; 3.30.1370.60; -; 1.
DR InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR InterPro; IPR003767; Malate/L-lactate_DH-like.
DR PANTHER; PTHR11091; PTHR11091; 1.
DR Pfam; PF02615; Ldh_2; 1.
DR SUPFAM; SSF89733; SSF89733; 1.
PE 3: Inferred from homology;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..361
FT /note="Hydroxycarboxylate dehydrogenase B"
FT /id="PRO_0000083841"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30178"
FT BINDING 122..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30178"
FT BINDING 178..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30178"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30178"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30178"
FT BINDING 313..316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30178"
SQ SEQUENCE 361 AA; 38884 MW; A3BB900DBA15EECE CRC64;
MESGHRFDAQ TLHSFIQAVF RQMGSEEQEA KLVADHLIAA NLAGHDSHGI GMIPSYVRSW
SQGHLQINHH AKIVKEAGAA VTLDGDRAFG QVAAHEAMAL GIEKAHQHGI AAVALHNSHH
IGRIGYWAEQ CAAAGFVSIH FVSVVGIPMV APFHGRDSRF GTNPFCVVFP RKDDFPLLLD
YATSAIAFGK TRVAWHKGVP VPPGCLIDVN GVPTTNPAVM QESPLGSLLT FAEHKGYALA
AMCEILGGAL SGGKTTHQET LQTSPDAILN CMTTIIINPE LFGAPDCSAQ TEAFAEWVKA
SPHDDDKPIL LPGEWEVNTR RERQEQGIPL DAGSWQAICD AARQIGMPEE TLQAFCQQLA
S
