GenomeNet

Database: UniProt
Entry: M7XCS9_RHOT1
LinkDB: M7XCS9_RHOT1
Original site: M7XCS9_RHOT1 
ID   M7XCS9_RHOT1            Unreviewed;       497 AA.
AC   M7XCS9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:EMS21594.1};
GN   ORFNames=RHTO_01654 {ECO:0000313|EMBL:EMS21594.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS21594.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS21594.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS21594.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {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; KB722655; EMS21594.1; -; Genomic_DNA.
DR   RefSeq; XP_016272713.1; XM_016415335.1.
DR   AlphaFoldDB; M7XCS9; -.
DR   GeneID; 27365667; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_1_0_1; -.
DR   OrthoDB; 1478027at2759; -.
DR   Proteomes; UP000016926; 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; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR43353:SF6; CYTOPLASMIC ALDEHYDE DEHYDROGENASE (EUROFUNG); 1.
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          33..484
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   497 AA;  53361 MW;  42746E89CA7EF4B0 CRC64;
     MSSSADSTSS QFLHAAPLPG LLNGKPFHGS ASYVVKDPHN PSKTLHQVSS ITVQDVPAVI
     DVAQKAFKSW KNSSVIERRN IFIRAGQILR ERIPELAKIE FEETTSSEGW AGFEMTLAAD
     SIEETAAAAT NALRGEIATT DSHQRAYIER CPYGVVLGMA PWNAPLTLCQ RAVLQPIMAG
     NTAILKTSEM SPRTHMILAE VMQQAGLPAG VLSIVHVAPE DAPGVVEAFI KHDAVGKVNF
     TGSTRVGSIV ASLCGKYIKP VVLELGGKAP AIVCEDADLE LAANAIKFGG LFHSGQICMA
     TQTAIVHESV VDKFLELLTD KYPRASADPT DGAALRGLFT TVSANRVKEI VDDALSKGAK
     IVAGEHKVEG NVVQPVLLAN VTEEMRVYRE EMFAPVFSVL TFSDYEKAIH YANDHDYGLA
     ASVFSKDIDR AYKLAKDVNA GLVHCNAPSV ADHPTIPHGG WKKSGFGRFN GLVGIREFCQ
     LKTITIDEKA TYPAPSA
//
DBGET integrated database retrieval system