ID A5DHI4_PICGU Unreviewed; 562 AA.
AC A5DHI4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=PGUG_02735 {ECO:0000313|EMBL:EDK38637.2};
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:EDK38637.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK38637.2, 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}.
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DR EMBL; CH408157; EDK38637.2; -; Genomic_DNA.
DR RefSeq; XP_001485006.1; XM_001484956.1.
DR AlphaFoldDB; A5DHI4; -.
DR STRING; 294746.A5DHI4; -.
DR GeneID; 5127282; -.
DR KEGG; pgu:PGUG_02735; -.
DR VEuPathDB; FungiDB:PGUG_02735; -.
DR eggNOG; KOG2456; Eukaryota.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; A5DHI4; -.
DR OMA; EPCIQGQ; -.
DR OrthoDB; 606537at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07135; ALDH_F14-YMR110C; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 542..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..488
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 562 AA; 61541 MW; 6D2F12C641840E58 CRC64;
MSKQSKNGAV AVPEGKKLKG SDSFHIVEKT LSTTSSNSVL TSTPLDEIEP NVARLHKQFH
SETNKLASVQ FRLNQLRNLY FAVKDNVDAI CDALRKDFGR AASESKNLEI APGLSELLHT
MSSLHKWIKP EKVTDVPLSM KSTPIYVERI PLGVILIITP FNYPFFLSLA PIAGAIAAGN
AVVFKPSELT PNYSALISKL FSEALDKDIF YVVNGGIPET TKVLEQKYDK IMYTGNNMVG
TIVAKKAAET LTPVILELGG KSPAIVLPDI TDKHLNTIAR RIVWGRFTNA GQTCVAVDYV
LVHESLKAKL VAEMKKVVQE QLYPNVNKND PSYTHIIHQR AYNNLKEVIK STKGEVVVGG
DTDDASRYIA PTIIDNVSWT DSSMKNELFG PILPVLSYKS LGDAIEGIIG NHDTPLAQYI
FTSSSTSRTA NKSVDQILRR VRSGATVVND VLLHVALVNA PFGGVGNSGH SNYHGWYSFR
AFTHERTIME QKLWNEGVLS VRYPPFNDKK DKAVSLSMDK YNGNVWFGRK GDVRIGGPST
FFGFWAGIAG VAALGAAVVS AL
//
