ID W6QTN9_PENRF Unreviewed; 348 AA.
AC W6QTN9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CDM32907.1};
GN ORFNames=PROQFM164_S02g003058 {ECO:0000313|EMBL:CDM32907.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM32907.1};
RN [1] {ECO:0000313|EMBL:CDM32907.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM32907.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; HG792016; CDM32907.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QTN9; -.
DR STRING; 1365484.W6QTN9; -.
DR OMA; WNHDLYK; -.
DR OrthoDB; 1111153at2759; -.
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:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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; 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 69..336
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 124..304
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 348 AA; 38202 MW; AD1CDB991A2999F9 CRC64;
MTKPIVLHLG DDIRWNHDQY SKFQDVFEIR RSYSMSRPEF IRALKERQFG DFFAIYRPFW
NTGGEMGNWD EELISLLPDS CKVYASAGAG FDWVDTAALA KKGVVYCNAA AACTESVADA
AIWLIISTFR LFSWSHIAAR ALDVDAFVDA NRNLAMVSHN PNGHTLGIIG FGQIGRRTAE
KAFLALNMKI HYYDIVQMPA QLEAVSKATY HKTMDSLLAV SDCVMVATPF SGETLLNASL
LAKMKDGSRL INIARGKLLD ESALVDALKS GKLAAAGLDV HYNEPRVSPE LASMKNVEMM
SHNAGASVDS HIGFERLGME NITAFYQTGK AVTPVNAHLV AKATGSKL
//
