ID A5DGL6_PICGU Unreviewed; 512 AA. AC A5DGL6; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 86. DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171}; GN ORFNames=PGUG_02417 {ECO:0000313|EMBL:EDK38319.1}; OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Meyerozyma. OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38319.1, ECO:0000313|Proteomes:UP000001997}; RN [1] {ECO:0000313|EMBL:EDK38319.1, ECO:0000313|Proteomes:UP000001997} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL RC Y-324 {ECO:0000313|Proteomes:UP000001997}; 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). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH408157; EDK38319.1; -; Genomic_DNA. DR RefSeq; XP_001484688.1; XM_001484638.1. DR AlphaFoldDB; A5DGL6; -. DR STRING; 294746.A5DGL6; -. DR GeneID; 5126721; -. DR KEGG; pgu:PGUG_02417; -. DR VEuPathDB; FungiDB:PGUG_02417; -. DR eggNOG; KOG2450; Eukaryota. DR HOGENOM; CLU_005391_0_1_1; -. DR InParanoid; A5DGL6; -. DR OMA; TWINTHM; -. DR OrthoDB; 216092at2759; -. DR Proteomes; UP000001997; 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 CDD; cd07091; ALDH_F1-2_Ald2-like; 1. 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:UP000001997}. FT DOMAIN 32..495 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 265 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 512 AA; 55506 MW; 26FD06D6CE453126 CRC64; MSVTIQSYGD CKITIKTGLF INNEFKPSVG GTVMTTPNPA TGEDLATISS ATAEDVDIAV SAARLAFETT WGKKSTPDQR SSLLNKWAEL IEADIDSLAE LESLDNGKPV WMARDVDIVD SIGCLRYYAG LADKIEGRTI EQQEGIKLAF TRAEPIGVCG QIIPWNYPIQ MFMWKVAPAL AAGNTIVIKP AEQTPLSALR LAELAVEAGF PPGVLNVVNG PGAVTGDAIS RHMDIDKVAF TGSTVTGRKI MEAAAKSNLK KVTLELGGKS PVVVFDSVDI DQTANWVCMA ILFNHGQDCC AGSRLFVQDT IKDEFLATLK KKVEQVEIGD PSVKTTFIGP LVSKQQQEKV KKYIQYGKDE GAVCLTGGED KLADLPQKFK NGFFVPPTVY TDCKKGMKIV DDEIFGPVLA VQTFETEEEA IELANDTAYG LGAGIFSQNA SQCMRMVHAI KAGTVWCNQY MVLSNAVPFG GMKQSGFGRE LGIEGLKEYT QTKAVHWNYG EEIEWPLNGT NV //