ID A1CP23_ASPCL Unreviewed; 335 AA.
AC A1CP23;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Hydroxyisocaproate dehydrogenase, putative {ECO:0000313|EMBL:EAW07394.1};
GN ORFNames=ACLA_021020 {ECO:0000313|EMBL:EAW07394.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07394.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07394.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW07394.1; -; Genomic_DNA.
DR RefSeq; XP_001268820.1; XM_001268819.1.
DR AlphaFoldDB; A1CP23; -.
DR STRING; 344612.A1CP23; -.
DR EnsemblFungi; EAW07394; EAW07394; ACLA_021020.
DR GeneID; 4701060; -.
DR KEGG; act:ACLA_021020; -.
DR VEuPathDB; FungiDB:ACLA_021020; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR OMA; TETCDSQ; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000006701; 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:SF284; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14400)-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 31..322
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 119..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 335 AA; 36450 MW; 455BA4A1F2F4FBD3 CRC64;
MPAALLIGAI THARKEWEDL AAILTLKEFP EGSRDDFIRN CKDGQYDDVL VIYRSNTSTK
FTGPFDSELL AVLPRSVKYI CHNGAGYDNI DIAGCSEKGI AVSSTPVAVN HATADVGIFL
MIGALRQAYV PLSALRAGQW QGKATLGHDP QGKVLGILGM GGIGREMANR AKAFGMKIQY
HNRSRLSPEL EGDAQYVSFD ELLANSDVLS LNLALNAHTR HIIGEKEFQK MKDGVVIVNT
ARGALIDEKA LVAALESGKV MSAGLDVYEN EPEIEAGLVN NPRVMLLPHI GTMTYETQKD
MELLVLNNLR SAVEKGEMIT LVPEQKDVFK GQNGQ
//
