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Database: UniProt
Entry: A1DN68_NEOFI
LinkDB: A1DN68_NEOFI
Original site: A1DN68_NEOFI 
ID   A1DN68_NEOFI            Unreviewed;       343 AA.
AC   A1DN68;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   20-JUN-2018, entry version 63.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:EAW16239.1};
GN   ORFNames=NFIA_055880 {ECO:0000313|EMBL:EAW16239.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16239.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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|RuleBase:RU003719}.
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DR   EMBL; DS027698; EAW16239.1; -; Genomic_DNA.
DR   RefSeq; XP_001258136.1; XM_001258135.1.
DR   ProteinModelPortal; A1DN68; -.
DR   STRING; 36630.CADNFIAP00004657; -.
DR   EnsemblFungi; EAW16239; EAW16239; NFIA_055880.
DR   GeneID; 4584651; -.
DR   KEGG; nfi:NFIA_055880; -.
DR   EuPathDB; FungiDB:NFIA_055880; -.
DR   HOGENOM; HOG000136700; -.
DR   OMA; STLEHIW; -.
DR   OrthoDB; EOG092C3I4U; -.
DR   Proteomes; UP000006702; 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   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006702};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT   DOMAIN       41    341       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      121    311       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
SQ   SEQUENCE   343 AA;  37497 MW;  36D5B175EA28D0BB CRC64;
     MSRIKFAILD DYQNLSRKHF AHLTFRVDIS YFPDTLDPRV PAQQQQLIAR LRPFDAILAM
     RERTPFNAAT IAALPNLKLL LTTGNRNLSL DLPALTARGI PVAGTVGRPP GVNSTVQHTW
     ALILALARHV ARDDAAVKAG KWQGSLGVNL SGKTLALLGL GKLGAQVGRI AVLAFGMRVI
     AWSANLTQEK ADEQATAQGL PAGSFEAVPE KGEFLRRADV LSVHYVLSER SRGIVGAEDL
     AALRPDAMIV NTSRGPLIDE RALLETLNAG RIRGAALDVF DPEPLPVDSP WRTTDWGVDG
     RSEVLLTPHM GYGEEELING WYKEAAENLE RWLDGKELQV RLN
//
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