ID H3NCU4_9LACT Unreviewed; 318 AA.
AC H3NCU4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9703_00375 {ECO:0000313|EMBL:EHR34767.1};
OS Dolosigranulum pigrum ATCC 51524.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Dolosigranulum.
OX NCBI_TaxID=883103 {ECO:0000313|EMBL:EHR34767.1, ECO:0000313|Proteomes:UP000003599};
RN [1] {ECO:0000313|EMBL:EHR34767.1, ECO:0000313|Proteomes:UP000003599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51524 {ECO:0000313|EMBL:EHR34767.1,
RC ECO:0000313|Proteomes:UP000003599};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dolosigranulum pigrum ATCC 51524.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHR34767.1}.
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DR EMBL; AGEF01000003; EHR34767.1; -; Genomic_DNA.
DR RefSeq; WP_004635109.1; NZ_JH601103.1.
DR AlphaFoldDB; H3NCU4; -.
DR STRING; 29394.BWX42_08455; -.
DR PATRIC; fig|883103.3.peg.375; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_9; -.
DR Proteomes; UP000003599; Unassembled WGS sequence.
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 CDD; cd12161; GDH_like_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000003599}.
FT DOMAIN 15..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 35190 MW; 99DEAC57FD7E05DA CRC64;
MKVALLEPLN VSKDLIDELA QPIEDLGHEF IYYPEKTTDR DELARRSEDA DIVMIANNPY
PREAFEHAKN LKLINVAFTG IDHVDQKTAK ELGIQIANAA GYSDQSVAEL VIGLALDVYR
QISGGNQAIR SDKFPGQVQG RELHGKTVGI IGTGNIGLKT AELFKAFGVT LIAYSRSERD
QAKELGIEYV ELDELMKRSD IITIHVPNND QTRGLISREK LELMSEDAIL INCARGPIVD
NEALAELLNE EKIAGVGLDV FDMEPPLPSD YPLLSAKNAI LTPHVAYLTD EAMINRAEIV
FDTTISYLKG EEKNIMVD
//
