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Database: UniProt
Entry: B8MG94_TALSN
LinkDB: B8MG94_TALSN
Original site: B8MG94_TALSN 
ID   B8MG94_TALSN            Unreviewed;       484 AA.
AC   B8MG94;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Vanillin dehydrogenase, putative {ECO:0000313|EMBL:EED16214.1};
DE            EC=1.2.1.16 {ECO:0000313|EMBL:EED16214.1};
GN   ORFNames=TSTA_013200 {ECO:0000313|EMBL:EED16214.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED16214.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; EQ962656; EED16214.1; -; Genomic_DNA.
DR   RefSeq; XP_002483448.1; XM_002483403.1.
DR   AlphaFoldDB; B8MG94; -.
DR   STRING; 441959.B8MG94; -.
DR   GeneID; 8108196; -.
DR   VEuPathDB; FungiDB:TSTA_013200; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_1_0_1; -.
DR   InParanoid; B8MG94; -.
DR   OMA; RQPCGVV; -.
DR   OrthoDB; 1478027at2759; -.
DR   PhylomeDB; B8MG94; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   CDD; cd07105; ALDH_SaliADH; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   DOMAIN          28..479
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   484 AA;  51670 MW;  AA4E794747B7E81C CRC64;
     MENGASVLGH VPVIPLLIDN ESIVTDVKFD VVSPLNNQCC YQSSSASVAE ANAAAQAAQA
     AFSQWTKLKP NVRRELLWKA ADLMDSVSDE LVRYQQEEMG ALPAAARRSI KRASDLLRDA
     GAMISLIEGT VPSLGQEGYA AVVLKEPYGV VLGIAPWNSP FILGMRAIAL PLAAGNTVIL
     KGSELSPKCF WALGQIFYRA GLPKGCVNVI FHRPSDAIEV TNSLIAHPAV QKINFTGSTQ
     VGRAIAAVAG KYGKPVLLEL GGKAPCIILD DADLQEAASG CLIGAFAGAG QICMSTERII
     VHRRVAESFR AILVEKAQEM FGASLPVPTL VSAASRKRIQ ILVSDALQKK AEKLFAPRDN
     KEQNDSQMQP IILENVSPDS DLYHTESFGP VASLFVVDSE GEAIELANDT EYGLTAAVYT
     NNLARGFMVA GQIQSGAVHI NSPTIHDEPV LPHGGVRSSG YGRFGGVHGL DEFLQTKVIT
     WKAD
//
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