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Database: UniProt
Entry: C5PG42_COCP7
LinkDB: C5PG42_COCP7
Original site: C5PG42_COCP7 
ID   C5PG42_COCP7            Unreviewed;       337 AA.
AC   C5PG42;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:EER23495.1};
GN   ORFNames=CPC735_048650 {ECO:0000313|EMBL:EER23495.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER23495.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER23495.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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:EER23495.1}.
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DR   EMBL; ACFW01000049; EER23495.1; -; Genomic_DNA.
DR   RefSeq; XP_003065640.1; XM_003065594.1.
DR   AlphaFoldDB; C5PG42; -.
DR   GeneID; 9691110; -.
DR   KEGG; cpw:CPC735_048650; -.
DR   VEuPathDB; FungiDB:CPC735_048650; -.
DR   HOGENOM; CLU_019796_1_2_1; -.
DR   OrthoDB; 1111153at2759; -.
DR   Proteomes; UP000009084; 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; cd12168; Mand_dh_like; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          37..331
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          126..300
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   337 AA;  36764 MW;  70FA28FAFE750913 CRC64;
     MGSDMRPKVL LLGKIDHAHT EWNALSDLAD LIEPRSTNRE DFIEECRSGG LDGVLVAYRT
     FGSVSITGLI DEELVNALPK SMRFLAHCGA GYDQIDVHAC SARSPPLLVS NVPTAVDDST
     ADVNMFLIIG TLRNFNTGMQ ALREGKWKGK PLPALGHDPQ GKTLGILGMG GIGRNLKKKA
     EAFGMKIIYH NRRKLSEELS DGAEYVSFDE LLAQSDVLSL NLPLNKNTQH IIGAPEFAKM
     KDGIIVVNTA RGAVMDEEAL VQALDSGKVL SAGLDVFEDE PNVHPGLLRN PNVMLVPHMG
     TWSVETQTAM EEWAMDNIRR VLETGKLKSP VPEQADM
//
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