ID A0A0A2KQB1_PENIT Unreviewed; 406 AA.
AC A0A0A2KQB1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding {ECO:0000313|EMBL:KGO66540.1};
GN ORFNames=PITC_012350 {ECO:0000313|EMBL:KGO66540.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO66540.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO66540.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO66540.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO66540.1}.
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DR EMBL; JQGA01001404; KGO66540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KQB1; -.
DR STRING; 40296.A0A0A2KQB1; -.
DR HOGENOM; CLU_019796_1_0_1; -.
DR OMA; WHHGTDK; -.
DR OrthoDB; 1775226at2759; -.
DR PhylomeDB; A0A0A2KQB1; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12163; 2-Hacid_dh_5; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 2.
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.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 119..188
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 227..322
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 406 AA; 44503 MW; 0F2BC7D5DCDCDCA2 CRC64;
MGDAPLPTEH VLVIFYPMMP EELKEVARQK FPDAEVTIYE VQPGVHVPPE VYQRATVLAT
FVDLPELKDS KNLKIVHTFS AGVDHLLQKP VLQETEIPIT TSSGIHGPPI AEWTVMNWLV
SSRKYVKGYE AQKSHSWDKS VYTPGVHDQV GKKVGILGYG SIGRQIARVS QALGMTVHAY
TATPRPTPES RRDTGYIIPG TGDPEGSIPA SWHHGTGREA IRSFLASGLD HLVVSLPLTP
QTTRLLGAEE FAILSENSNH HTSKPYVTNI SRGKVIDQKA LVDALNSGVL SGAALDVTDP
EPLPKDDPLW EASNVQISPH VSGLGVEYFP RSLDILAVNL EHIARGIGCN NATRLDKPWM
HCVKSESISL HNFIGALSLF EQILKDISQV ALNPTWTFDL LGLRPL
//
