ID D5GBF0_TUBMM Unreviewed; 449 AA.
AC D5GBF0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=GSTUM_00000440001 {ECO:0000313|EMBL:CAZ81843.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ81843.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ81843.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ81843.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; FN430093; CAZ81843.1; -; Genomic_DNA.
DR RefSeq; XP_002837652.1; XM_002837606.1.
DR AlphaFoldDB; D5GBF0; -.
DR STRING; 656061.D5GBF0; -.
DR EnsemblFungi; CAZ81843; CAZ81843; GSTUM_00000440001.
DR GeneID; 9184416; -.
DR KEGG; tml:GSTUM_00000440001; -.
DR eggNOG; KOG2451; Eukaryota.
DR HOGENOM; CLU_005391_5_3_1; -.
DR InParanoid; D5GBF0; -.
DR OMA; CFRFKTE; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000006911; 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; 2.
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:UP000006911}.
FT DOMAIN 29..295
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 299..439
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 449 AA; 48720 MW; 54CDCDE8E0632F5F CRC64;
MPLSSHIVPK LKDPSLFHEA AFINGQFVKA KDGKTFDDSI NIARDALKSF RKTLPRERAR
MLRKWYELIM ENQEDLATLI TRENGKPLAD ARSEVAYAAA FFEWFSEEAP RIYGDSIPAS
VRGNRVVTVK QPVGVCGLIT PWNFPAAMIT RKIGPALAAG CTVVAKAPGE TPLTSLAIAE
LASRAGIPKG VVNIVTALKN TPEIGRELCT NPIIKKVSFT GSTSVGKLLM QQCSSTLKKL
SLELGGNAPF IVFDDADLDK AVAGAIISKF RSSGQTCVCT NRIYVQDAVY SEFQRESFKF
QTHVEDALKK GATVLTGGKG LGHLGPNFYE PTVITNMTSD MRIHREETFG PVAALFRFKS
EKEVVNLANE AEVGLAGYFF SSDIARIWRV AEALEVGMVG VNTGLISDAA SPFGGVKESG
FGREGSKYGI DEYTIIKSIT FGGVDDLQE
//