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Database: UniProt
Entry: F9G8E9_FUSOF
LinkDB: F9G8E9_FUSOF
Original site: F9G8E9_FUSOF 
ID   F9G8E9_FUSOF            Unreviewed;       507 AA.
AC   F9G8E9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=FOXB_14931 {ECO:0000313|EMBL:EGU74558.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU74558.1};
RN   [1] {ECO:0000313|EMBL:EGU74558.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU74558.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU74558.1}.
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DR   EMBL; AFQF01003662; EGU74558.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9G8E9; -.
DR   STRING; 660025.F9G8E9; -.
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}.
FT   DOMAIN          37..503
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   507 AA;  54858 MW;  A2E1877C5EBE7DBE CRC64;
     MTRTPLFKKE IPYVVTRNFQ FRDPSLVDTK AFIGGKWVPA ASGQMFKILD PEDDTEVCEV
     ADLNAHDTRK AVEAASKAFE TYKLTPHRER RWLMRRWGDL IRAAKDDLAA LCTLELGKPF
     TESLTTVQYA LDFIDHFETG IERTYGETIP AARGNNRILT IREPQGVVAC ITPWNSPVAM
     VTRKVGAALA AGNTVVCKPA PETPLCAIAL AKLFERAGGP PGVFNIVTAG QENTPAVGEE
     FCKNPAIKHL SFTGSTTIGR LLNVQCAKTI KKTSLELGGN AAFIVFEDAD LKKAANGVIA
     SKFRSSGQTC VCANRIYVHS SIMDAFADTL SDTLKATFVY GSVWDAKVNF GPLYSGKGLA
     KVEAHLQDAI QQGSRVSYRG TVDNLGPNFF PPTVVVVPRG ETLMMKFLTE ETFGPLAFLV
     PFDSEEEVVR LANATDVGLA AYFFTESISR VWRVSEALKV GMVGVGVGLV SAAEQPFGGV
     LESGLGREGG PAALEEYLDI KSITVGI
//
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