HCXA_ECOLI
ID HCXA_ECOLI Reviewed; 362 AA.
AC P45579; P77632;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Hydroxycarboxylate dehydrogenase A {ECO:0000303|PubMed:27941785};
DE EC=1.1.1.- {ECO:0000269|PubMed:27941785};
DE AltName: Full=2-oxobutanoate reductase {ECO:0000305|PubMed:27941785};
DE AltName: Full=2-oxoglutarate reductase {ECO:0000305|PubMed:27941785};
GN Name=hcxA {ECO:0000303|PubMed:27941785};
GN Synonyms=ybdH {ECO:0000312|EMBL:AAC73700.1};
GN OrderedLocusNames=b0599, JW0592;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-362.
RC STRAIN=K12;
RX PubMed=1848300; DOI=10.1016/0022-2836(91)90879-b;
RA Schultz J.E., Matin A.;
RT "Molecular and functional characterization of a carbon starvation gene of
RT Escherichia coli.";
RL J. Mol. Biol. 218:129-140(1991).
RN [6]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 2-oxoglutarate and
CC 2-oxobutanoate, leading to the respective 2-hydroxycarboxylate. Cannot
CC use NADH instead of NADPH as a redox partner. Do not catalyze the
CC reverse reactions. {ECO:0000269|PubMed:27941785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxybutanoate + NADP(+) = 2-oxobutanoate + H(+) + NADPH;
CC Xref=Rhea:RHEA:52608, ChEBI:CHEBI:15378, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64552;
CC Evidence={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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O13702};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O13702};
CC -!- INTERACTION:
CC P45579; P45579: hcxA; NbExp=3; IntAct=EBI-553586, EBI-553586;
CC P45579; P0AFT8: yeiW; NbExp=3; IntAct=EBI-553586, EBI-8767954;
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a consistent change
CC in 2-hydroxyglutarate level. {ECO:0000269|PubMed:27941785}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U82598; AAB40800.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73700.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35229.1; -; Genomic_DNA.
DR EMBL; X52904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64793; E64793.
DR RefSeq; NP_415132.1; NC_000913.3.
DR RefSeq; WP_001120441.1; NZ_SSZK01000032.1.
DR AlphaFoldDB; P45579; -.
DR SMR; P45579; -.
DR BioGRID; 4259892; 12.
DR BioGRID; 849597; 7.
DR DIP; DIP-11347N; -.
DR IntAct; P45579; 11.
DR STRING; 511145.b0599; -.
DR PaxDb; P45579; -.
DR PRIDE; P45579; -.
DR EnsemblBacteria; AAC73700; AAC73700; b0599.
DR EnsemblBacteria; BAA35229; BAA35229; BAA35229.
DR GeneID; 945212; -.
DR KEGG; ecj:JW0592; -.
DR KEGG; eco:b0599; -.
DR PATRIC; fig|1411691.4.peg.1669; -.
DR EchoBASE; EB2555; -.
DR eggNOG; COG0371; Bacteria.
DR HOGENOM; CLU_044754_2_0_6; -.
DR InParanoid; P45579; -.
DR OMA; HCSERDV; -.
DR PhylomeDB; P45579; -.
DR BioCyc; EcoCyc:EG12692-MON; -.
DR PRO; PR:P45579; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; PTHR43616; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..362
FT /note="Hydroxycarboxylate dehydrogenase A"
FT /id="PRO_0000087831"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O13702"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O13702"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O13702"
SQ SEQUENCE 362 AA; 39092 MW; C28BBB4F8F247AE2 CRC64;
MPHNPIRVVV GPANYFSHPG SFNHLHDFFT DEQLSRAVWI YGKRAIAAAQ TKLPPAFGLP
GAKHILFRGH CSESDVQQLA AESGDDRSVV IGVGGGALLD TAKALARRLG LPFVAVPTIA
ATCAAWTPLS VWYNDAGQAL HYEIFDDANF MVLVEPEIIL NAPQQYLLAG IGDTLAKWYE
AVVLAPQPET LPLTVRLGIN NAQAIRDVLL NSSEQALSDQ QNQQLTQSFC DVVDAIIAGG
GMVGGLGDRF TRVAAAHAVH NGLTVLPQTE KFLHGTKVAY GILVQSALLG QDDVLAQLTG
AYQRFHLPTT LAELEVDINN QAEIDKVIAH TLRPVESIHY LPVTLTPDTL RAAFKKVESF
KA
