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
//