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Database: UniProt
Entry: K9EAT3_9LACT
LinkDB: K9EAT3_9LACT
Original site: K9EAT3_9LACT 
ID   K9EAT3_9LACT            Unreviewed;       318 AA.
AC   K9EAT3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9698_01534 {ECO:0000313|EMBL:EKU92931.1};
OS   Alloiococcus otitis ATCC 51267.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alloiococcus.
OX   NCBI_TaxID=883081 {ECO:0000313|EMBL:EKU92931.1, ECO:0000313|Proteomes:UP000009875};
RN   [1] {ECO:0000313|EMBL:EKU92931.1, ECO:0000313|Proteomes:UP000009875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51267 {ECO:0000313|EMBL:EKU92931.1,
RC   ECO:0000313|Proteomes:UP000009875};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Alloiococcus otitis ATCC 51267.";
RL   Submitted (SEP-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:EKU92931.1}.
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DR   EMBL; AGXA01000031; EKU92931.1; -; Genomic_DNA.
DR   RefSeq; WP_003779072.1; NZ_JH992962.1.
DR   AlphaFoldDB; K9EAT3; -.
DR   STRING; 883081.HMPREF9698_01534; -.
DR   PATRIC; fig|883081.3.peg.1539; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_3_9; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000009875; 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; 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   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   PANTHER; PTHR43761:SF1; 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.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009875}.
FT   DOMAIN          20..312
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;  34740 MW;  72EA6B41B91188E5 CRC64;
     MKVSLLEPLN VSQNLIDRLA QPIKDLGHDF VYYSDQTSDP EELADRTGDS DIVMIANTPY
     PKQAFSQADK LQLINVAFTG IDHVDQEAAR EKGIKIANAA GYSDQSVAEH VIGLILDLYR
     QISWGNQAIR QSNFPGPSQG RVLAGKTVGI IGTGNIGLKT ASLLKAFGVQ FLAYSRTEKD
     QAKAMGVKYV SLERLLEESD IVTVHLPHND QTQGLLSKDK LALMKDTAIL INCARGPIVD
     NDGLADLLNQ GQLAGAGIDV FDREPPLPED YKLLQAQNTI LTPHVAYLTD QAMVNRAKIV
     FDTTLAYLKG EEKNIQLG
//
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