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Database: UniProt
Entry: A0A0D2HJX3_9EURO
LinkDB: A0A0D2HJX3_9EURO
Original site: A0A0D2HJX3_9EURO 
ID   A0A0D2HJX3_9EURO        Unreviewed;       459 AA.
AC   A0A0D2HJX3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00019842};
DE            EC=1.2.1.24 {ECO:0000256|ARBA:ARBA00013051};
DE   AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00030806};
GN   ORFNames=Z517_00197 {ECO:0000313|EMBL:KIW84809.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW84809.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW84809.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW84809.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; KN846969; KIW84809.1; -; Genomic_DNA.
DR   RefSeq; XP_013288617.1; XM_013433163.1.
DR   AlphaFoldDB; A0A0D2HJX3; -.
DR   STRING; 1442368.A0A0D2HJX3; -.
DR   GeneID; 25299687; -.
DR   VEuPathDB; FungiDB:Z517_00197; -.
DR   HOGENOM; CLU_005391_5_3_1; -.
DR   OrthoDB; 216092at2759; -.
DR   Proteomes; UP000053029; 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; cd07103; ALDH_F5_SSADH_GabD; 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; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT   DOMAIN          32..453
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   459 AA;  49888 MW;  32470CCB88036B3D CRC64;
     MGSLGSFQQT KSLADVKNKK LLHYKGFIDG QWADAASGKT FDLIDPGTGE KLATFPEMGA
     ADVARAIDSA SKTFVTWKNT SGRDRARMLR KWNDLCLENT EDFALIITLE TGKPLYEARA
     EVIYACSFLE WFAGEAERTH GENILTANRK QRLVTMKQPI GVVGCLMPWN YPMAMITRKA
     SAAIAAGCTT IWKPAGETPL SAGAMAVLAM EAGIPAGVIQ IITSLTTVAE VGKEICTNKL
     VKKVSFTGST RVGRLLMEQC APTVKKLSLE LGGNSPFIVF DDADVDVAVE AAVMAKFRNT
     GQTCVAANRI FVQDGIYDRF AKALSNTIST FKIGPGTQDG VFVGPLTHEN VLSKVLTHIE
     EAKNNGGKII LGGNRVEGTK GYYVQPTIIA DMPRGTITER DEVFGPVIPL YRFHTEEEVI
     ELANNVDVGL GAFVMTSSMP RQWRVTEALE ASCFFPCLY
//
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