ID A1CLR8_ASPCL Unreviewed; 360 AA.
AC A1CLR8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=NAD dependent epimerase/dehydratase {ECO:0000313|EMBL:EAW09047.1};
GN ORFNames=ACLA_077940 {ECO:0000313|EMBL:EAW09047.1};
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:EAW09047.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09047.1, 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 NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily.
CC {ECO:0000256|ARBA:ARBA00023445}.
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DR EMBL; DS027057; EAW09047.1; -; Genomic_DNA.
DR RefSeq; XP_001270473.1; XM_001270472.1.
DR AlphaFoldDB; A1CLR8; -.
DR STRING; 344612.A1CLR8; -.
DR EnsemblFungi; EAW09047; EAW09047; ACLA_077940.
DR GeneID; 4702561; -.
DR KEGG; act:ACLA_077940; -.
DR VEuPathDB; FungiDB:ACLA_077940; -.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_2_1; -.
DR OMA; FDYIIHT; -.
DR OrthoDB; 1200131at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10366:SF814; EPIMERASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 10..277
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 360 AA; 39489 MW; 41F8744D4FE3DF01 CRC64;
MTSSVNSQHV LLTGANGFVA SHILSILIER GFAVTATVRS QAKADDIITT HPSWKGKITF
ALVSDFTSQQ PFDELFANTT VPFTHVIHTA SPVKFNVQDI QKEMIEPAVM GTTEILKSAH
RHGGPALKRF VLLSSAATVL DSFEDLTREG PPYTEKDWNP VTAQQAIDRK DIVLGYNVSK
IQGEQTAWAF METNNPDFDL TVINPVVITG PMAHPISGPG SINETNHFAI ASFIDGTHTT
VEDVRFPFWH FVDVRDVARS HVDALTNPAA GGQRIVLIAG LLTPQLVVNI IRKNFPGLRD
RVPEGNPSQI LPAGVHPNDW DTRLSLDVLS KGTADGRWEY IELEKSVTDA VQSMIDQKVL
//
