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Database: UniProt
Entry: W6MM22_9ASCO
LinkDB: W6MM22_9ASCO
Original site: W6MM22_9ASCO 
ID   W6MM22_9ASCO            Unreviewed;       497 AA.
AC   W6MM22;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN   ORFNames=KUCA_T00003529001 {ECO:0000313|EMBL:CDK27551.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK27551.1};
RN   [1] {ECO:0000313|EMBL:CDK27551.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK27551.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK27551.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK27551.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; HG793128; CDK27551.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MM22; -.
DR   STRING; 1382522.W6MM22; -.
DR   HOGENOM; CLU_005391_1_0_1; -.
DR   OrthoDB; 216092at2759; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          33..489
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   497 AA;  53719 MW;  BF21716D85C98A51 CRC64;
     MSLSTTIKLP NGKEYEQPLG LFIGGEYITP EVDSKITVIN PSNEEVITEV YAGDKADIDK
     AVVAARKAFE SPEWRGIAAS ARGDYLYKIA QIIDRDRELI ASIDSIDNGK PLPECVEGDL
     EEAYNVFKYY AGFADKITGK TIETSPEKLA YTVQEPLGVC GQIIPWNYPF MMLAWKVAPA
     LCCGNTVILK PSEVTPLSAL YFGKICQEAG LPAGVVNVVN GYGKTAGAAL SEHTGVDKIA
     FTGSTASGKL IMKAAANNLK NVTLECGGKN PLIIFDDAEL DQAVKWARIG IFDNKGEVCT
     STSRIYVQEA IYDKFLEEFV AHIKDVTVVA DPFGENTTQG PQVSKMQYEK VLSYIESGKA
     EGAKLAYGGA KASEKGYFLN PTVFSDVQED MKINKEEIFG PVVAVSKFST VEEVVQKAND
     TSYGLAAALF SQNVTQCVTV ASKLQAGMVW INSNNDSHFG IPFGGYKSSG IGRELGPYAL
     DAYTQTKAVH INVGLRV
//
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