ID C5M650_CANTT Unreviewed; 287 AA.
AC C5M650;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:EER34469.1, ECO:0000313|EMBL:EER34475.1};
GN ORFNames=CTRG_01331 {ECO:0000313|EMBL:EER34469.1}, CTRG_01335
GN {ECO:0000313|EMBL:EER34475.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34469.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER34469.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037}, and
RC MYA-3404 {ECO:0000313|EMBL:EER34469.1};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|EMBL:EER34469.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MYA-3404 {ECO:0000313|EMBL:EER34469.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C.,
RA Kellis M., Rasmussen M.D., Grochow J.A., Jaffe D., Butler J., Alvarez P.,
RA Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W., MacCallum I.A.,
RA Rounsley S., Young S., LaButti K., Pushparaj V., DeCaprio D., Crawford M.,
RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L.,
RA Luoma S., White J., Zeng Q., Kodira C., Yandava C., Alvarado L.,
RA O'Leary S., Soll D.R., Srikantha T.;
RL Submitted (JUN-2009) 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; GG692396; EER34469.1; -; Genomic_DNA.
DR EMBL; GG692396; EER34475.1; -; Genomic_DNA.
DR RefSeq; XP_002547024.1; XM_002546978.1.
DR RefSeq; XP_002547030.1; XM_002546984.1.
DR AlphaFoldDB; C5M650; -.
DR STRING; 294747.C5M650; -.
DR EnsemblFungi; CTRG_01331-t43_1; CTRG_01331-t43_1-p1; CTRG_01331.
DR EnsemblFungi; CTRG_01335-t43_1; CTRG_01335-t43_1-p1; CTRG_01335.
DR GeneID; 8301059; -.
DR GeneID; 8301062; -.
DR KEGG; ctp:CTRG_01331; -.
DR KEGG; ctp:CTRG_01335; -.
DR VEuPathDB; FungiDB:CTRG_01331; -.
DR VEuPathDB; FungiDB:CTRG_01335; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_1_4_1; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
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; IPR016160; Ald_DH_CS_CYS.
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; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 1..279
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 287 AA; 30680 MW; B52AA8F0B319997C CRC64;
MPKGVVNIVP GFGATTGAAI ASHPKIDKVA FTGSTATGKV IMKLAAESNL KKVTLELGGK
SPNIVFNDAD LDKTIDNLVV SIFYNSGEVC CAGSRLLVQS GVYDEVVARF KKAAESLKVG
DPFEEDTFMG SQANANQLDK ILKYIEVGKE QGATVVTGGA KASDKGYFIK PTIFADVNKD
MSIVKEEIFG PVVTLIKFDT VEEAIALAND SDYGLAAGIH STDVNKCIDV SNRLKAGTVW
VNTYNDFHPM VPFGGFSASG IGREMGEEVL KEYTQVRAVR MKLNPLP
//
