HCXB_ECOLI
ID HCXB_ECOLI Reviewed; 361 AA.
AC P30178; P75778;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Hydroxycarboxylate dehydrogenase B {ECO:0000303|PubMed:27941785};
DE EC=1.1.1.- {ECO:0000269|PubMed:27941785};
DE AltName: Full=2-oxoglutarate reductase {ECO:0000305|PubMed:27941785};
DE AltName: Full=Hydroxyphenylpyruvate reductase {ECO:0000305|PubMed:27941785};
DE EC=1.1.1.237 {ECO:0000269|PubMed:27941785};
DE AltName: Full=Phenylpyruvate reductase {ECO:0000305|PubMed:27941785};
GN Name=hcxB {ECO:0000303|PubMed:27941785};
GN Synonyms=ybiC {ECO:0000312|EMBL:AAC73888.1};
GN OrderedLocusNames=b0801, JW0786;
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;
RX PubMed=8037924; DOI=10.1266/jjg.69.1;
RA Ohmori H.;
RT "Structural analysis of the rhlE gene of Escherichia coli.";
RL Jpn. J. Genet. 69:1-12(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=27941785; DOI=10.1038/nmeth.4103;
RA Sevin D.C., Fuhrer T., Zamboni N., Sauer U.;
RT "Nontargeted in vitro metabolomics for high-throughput identification of
RT novel enzymes in Escherichia coli.";
RL Nat. Methods 14:187-194(2017).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH NAD.
RA Cuff M.E., Skarina T., Edwards A., Savchenko A., Cymborowski M., Minor W.,
RA Joachimiak A.;
RT "The structure of a putative malate/lactate dehydrogenase from E. coli.";
RL Submitted (MAR-2006) to the PDB data bank.
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:0000269|PubMed:27941785}.
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; L02123; AAA53657.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73888.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35467.1; -; Genomic_DNA.
DR PIR; A64817; A64817.
DR RefSeq; NP_415322.1; NC_000913.3.
DR RefSeq; WP_000443530.1; NZ_STEB01000019.1.
DR PDB; 2G8Y; X-ray; 2.15 A; A/B=1-361.
DR PDBsum; 2G8Y; -.
DR AlphaFoldDB; P30178; -.
DR SMR; P30178; -.
DR BioGRID; 4259966; 10.
DR BioGRID; 849786; 1.
DR DIP; DIP-11426N; -.
DR STRING; 511145.b0801; -.
DR jPOST; P30178; -.
DR PaxDb; P30178; -.
DR PRIDE; P30178; -.
DR EnsemblBacteria; AAC73888; AAC73888; b0801.
DR EnsemblBacteria; BAA35467; BAA35467; BAA35467.
DR GeneID; 945412; -.
DR KEGG; ecj:JW0786; -.
DR KEGG; eco:b0801; -.
DR PATRIC; fig|1411691.4.peg.1477; -.
DR EchoBASE; EB1541; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_1_0_6; -.
DR InParanoid; P30178; -.
DR OMA; HDIGMAS; -.
DR PhylomeDB; P30178; -.
DR BioCyc; EcoCyc:EG11581-MON; -.
DR BioCyc; MetaCyc:EG11581-MON; -.
DR EvolutionaryTrace; P30178; -.
DR PRO; PR:P30178; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..361
FT /note="Hydroxycarboxylate dehydrogenase B"
FT /id="PRO_0000083840"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:2G8Y"
FT BINDING 122..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:2G8Y"
FT BINDING 178..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:2G8Y"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:2G8Y"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:2G8Y"
FT BINDING 313..316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:2G8Y"
FT CONFLICT 23..24
FT /note="MG -> IP (in Ref. 1; AAA53657)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 90..108
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2G8Y"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:2G8Y"
FT TURN 247..252
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:2G8Y"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:2G8Y"
FT HELIX 349..360
FT /evidence="ECO:0007829|PDB:2G8Y"
SQ SEQUENCE 361 AA; 38897 MW; 2B29784979E48543 CRC64;
MESGHRFDAQ TLHSFIQAVF RQMGSEEQEA KLVADHLIAA NLAGHDSHGI GMIPSYVRSW
SQGHLQINHH AKTVKEAGAA VTLDGDRAFG QVAAHEAMAL GIEKAHQHGI AAVALHNSHH
IGRIGYWAEQ CAAAGFVSIH FVSVVGIPMV APFHGRDSRF GTNPFCVVFP RKDNFPLLLD
YATSAIAFGK TRVAWHKGVP VPPGCLIDVN GVPTTNPAVM QESPLGSLLT FAEHKGYALA
AMCEILGGAL SGGKTTHQET LQTSPDAILN CMTTIIINPE LFGAPDCNAQ TEAFAEWVKA
SPHDDDKPIL LPGEWEVNTR RERQKQGIPL DAGSWQAICD AARQIGMPEE TLQAFCQQLA
S
