ID S2ZHV8_BIFBR Unreviewed; 338 AA.
AC S2ZHV8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1482_01163 {ECO:0000313|EMBL:EPD75991.1};
OS Bifidobacterium breve HPH0326.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1203540 {ECO:0000313|EMBL:EPD75991.1, ECO:0000313|Proteomes:UP000014395};
RN [1] {ECO:0000313|EMBL:EPD75991.1, ECO:0000313|Proteomes:UP000014395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPH0326 {ECO:0000313|EMBL:EPD75991.1,
RC ECO:0000313|Proteomes:UP000014395};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dover J., Dai D.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bifidobacterium breve HPH0326.";
RL Submitted (MAY-2013) 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:EPD75991.1}.
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DR EMBL; ATCB01000002; EPD75991.1; -; Genomic_DNA.
DR RefSeq; WP_016462591.1; NZ_KE150454.1.
DR AlphaFoldDB; S2ZHV8; -.
DR GeneID; 69564859; -.
DR PATRIC; fig|1203540.3.peg.1154; -.
DR HOGENOM; CLU_019796_1_3_11; -.
DR Proteomes; UP000014395; 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; cd12169; PGDH_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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 32..335
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 129..304
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 338 AA; 36692 MW; E737EECAB2E12480 CRC64;
MTEIYETQSE RTDLPLVVMP AVLDAMIEPI KAQFPALHDV ARVRMFEEFT SDEAVLAERL
KNADALLVGG YHISDDLLRT ISEQGHVKCI VFCGTGVASY INLELARELK VRVCNAEHYG
DHAVAEHTFA LLFELIRKVG QLDKDVKAGN WAWAGGDGLQ LAGRRMGIIG LGGIGTTVAG
IARAFGMEVA AWNSHVPAEH FERSGAVPVD DLNELIETSD VISVHLPLND ATRGIVTAEN
LAHLKPGTML INTARSEVIE SGALLARLQE GDIPAALDVF DHEPLAADDP ICHVPGIVLT
PHVGWRTDGA FKELTRQMIA CMNAYFAGED YNVAVSEH
//
