HADHA_ASPOR
ID HADHA_ASPOR Reviewed; 347 AA.
AC Q2UH56;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=2-hydroxyacid dehydrogenase A {ECO:0000303|PubMed:26615399};
DE Short=2-HadhA {ECO:0000303|PubMed:26615399};
DE EC=1.1.1.272 {ECO:0000269|PubMed:26615399};
GN ORFNames=AO090023000577;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26615399; DOI=10.1007/s00253-015-7182-0;
RA Shimizu M., Yamamoto T., Okabe N., Sakai K., Koide E., Miyachi Y.,
RA Kurimoto M., Mochizuki M., Yoshino-Yasuda S., Mitsui S., Ito A., Murano H.,
RA Takaya N., Kato M.;
RT "Novel 4-methyl-2-oxopentanoate reductase involved in synthesis of the
RT Japanese sake flavor, ethyl leucate.";
RL Appl. Microbiol. Biotechnol. 100:3137-3145(2016).
CC -!- FUNCTION: 2-hydroxyacid dehydrogenase that is capable to reduce
CC pyruvate, hydroxypyruvate and glyoxylate in a NADPH- or NADH-dependent
CC manner (PubMed:26615399). In contrast to 2-HadhD/morA, does not
CC recognize 4-methyl-2-oxopentanoate (MOA) as a substrate
CC (PubMed:26615399). {ECO:0000269|PubMed:26615399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2R)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate +
CC H(+) + NADPH; Xref=Rhea:RHEA:35735, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:35179, ChEBI:CHEBI:57783, ChEBI:CHEBI:58314,
CC ChEBI:CHEBI:58349; EC=1.1.1.272;
CC Evidence={ECO:0000269|PubMed:26615399};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35737;
CC Evidence={ECO:0000269|PubMed:26615399};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.66 mM for pyruvate {ECO:0000269|PubMed:26615399};
CC KM=6.3 mM for hydroxypyruvate {ECO:0000269|PubMed:26615399};
CC KM=43.0 mM for glyoxylate {ECO:0000269|PubMed:26615399};
CC Note=kcat is 14.0 sec(-1) with pyruvate as substrate. kcat is 170.0
CC sec(-1) with hydroxypyruvate as substrate. kcat is 591.0 sec(-1) with
CC glyoxylate as substrate. {ECO:0000269|PubMed:26615399};
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AP007157; BAE59109.1; -; Genomic_DNA.
DR RefSeq; XP_001821111.1; XM_001821059.1.
DR SMR; Q2UH56; -.
DR STRING; 510516.Q2UH56; -.
DR EnsemblFungi; BAE59109; BAE59109; AO090023000577.
DR GeneID; 5993113; -.
DR KEGG; aor:AO090023000577; -.
DR VEuPathDB; FungiDB:AO090023000577; -.
DR HOGENOM; CLU_019796_1_1_1; -.
DR OMA; VIVTAHQ; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..347
FT /note="2-hydroxyacid dehydrogenase A"
FT /id="PRO_0000455828"
FT ACT_SITE 236
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT ACT_SITE 265
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT BINDING 157..158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT BINDING 234..236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
SQ SEQUENCE 347 AA; 37997 MW; E07145E7A878338B CRC64;
MKLAVFSAKS YDKHYFDATL RKHHPALCEI TYHSFALSSE TVSLAQDSDA VCVFVNDQLD
APVLETLYAN GVRAILLRCA GFNNINLQVA EDLGFFVANV PSYSPEAVAE FAVALIQTLN
RKTHRAFNRV REGNFNLEGF LGRTLYGKTV GVVGVGRIGL AFAKILHGFG CKLVAYDPFG
GEEFKKYGEF VELGDLLAQS DVVSLHCPLT EGTRHVINDE NLGRMKKGAL LVNTSRGGLV
NTKAVINALK SGQLGGVALD VYEEEGALFY NDHSGEIIHD DVLMRLMTFP NVLVCGHQAF
FTEEALSEIA GVTLGNLEDF VLKRTCKNSL VREGHLVVPT DKEPVRL
