DDH2_SCHPO
ID DDH2_SCHPO Reviewed; 332 AA.
AC Q9P7Q1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=2-hydroxyacid dehydrogenase homolog 2;
DE EC=1.1.1.-;
GN ORFNames=SPAC186.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB75866.1; -; Genomic_DNA.
DR PIR; T50129; T50129.
DR RefSeq; NP_595020.1; NM_001020451.2.
DR AlphaFoldDB; Q9P7Q1; -.
DR SMR; Q9P7Q1; -.
DR STRING; 4896.SPAC186.02c.1; -.
DR PaxDb; Q9P7Q1; -.
DR PRIDE; Q9P7Q1; -.
DR EnsemblFungi; SPAC186.02c.1; SPAC186.02c.1:pep; SPAC186.02c.
DR GeneID; 2542495; -.
DR KEGG; spo:SPAC186.02c; -.
DR PomBase; SPAC186.02c; -.
DR VEuPathDB; FungiDB:SPAC186.02c; -.
DR eggNOG; KOG0068; Eukaryota.
DR HOGENOM; CLU_019796_1_1_1; -.
DR InParanoid; Q9P7Q1; -.
DR OMA; VIVTAHQ; -.
DR PhylomeDB; Q9P7Q1; -.
DR PRO; PR:Q9P7Q1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..332
FT /note="2-hydroxyacid dehydrogenase homolog 2"
FT /id="PRO_0000316031"
FT ACT_SITE 235
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /evidence="ECO:0000250"
FT ACT_SITE 296
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 233..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 296..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 36369 MW; F886902386782C40 CRC64;
MRVVLFSSQS YDRGPFEEAN KTFNHEIIYH NFSLNKDTVS LAGKAQVVCV FVNDQVDADT
LKALAENGVK LVALRCGGYN NVNLKAASEY KITVVHVPSY SPFAVSEFTV GLLLSLNRKI
HRAYVRVRED DFNIVGLLGC DIHGKTVGVI GTGKIGSNVA KCFKMGFGCD VLAYDINPDK
KLENYGVQFV EQNEVLKKAD FLCLHCPLTP STTHIVNSDS LALMKKGVTI VNTSRGGLID
TKALVDAIDS GQVGGCAIDV YEGERNLFYK DLSNEVIKDS TFQRLVNFPN VLVTSHQAFF
TTEALCSIAH TTLKSASDFY TNSLDESVIA NK