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Database: UniProt
Entry: A0A101XTV1_9BACL
LinkDB: A0A101XTV1_9BACL
Original site: A0A101XTV1_9BACL 
ID   A0A101XTV1_9BACL        Unreviewed;       491 AA.
AC   A0A101XTV1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=NAD-dependent succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KUO97345.1};
GN   Name=gabD {ECO:0000313|EMBL:KUO97345.1};
GN   ORFNames=ATW55_04655 {ECO:0000313|EMBL:KUO97345.1};
OS   Ferroacidibacillus organovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Ferroacidibacillus.
OX   NCBI_TaxID=1765683 {ECO:0000313|EMBL:KUO97345.1, ECO:0000313|Proteomes:UP000053557};
RN   [1] {ECO:0000313|EMBL:KUO97345.1, ECO:0000313|Proteomes:UP000053557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITV001 {ECO:0000313|EMBL:KUO97345.1,
RC   ECO:0000313|Proteomes:UP000053557};
RA   Dall'Agnol H., Nancucheo I., Johnson B., Oliveira R., Leite L., Pylro V.,
RA   Nunes G.L., Tzotzos G., Fernandes G.R., Dutra J., Orellana S.C.,
RA   Oliveira G.;
RT   "Draft genome sequence of Acidibacillus ferrooxidans ITV001, isolated from
RT   a chalcopyrite acid mine drainage site in Brazil.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, 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:KUO97345.1}.
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DR   EMBL; LPVJ01000002; KUO97345.1; -; Genomic_DNA.
DR   RefSeq; WP_067711164.1; NZ_LPVJ01000002.1.
DR   AlphaFoldDB; A0A101XTV1; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000053557; 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}.
FT   DOMAIN          25..487
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   491 AA;  52148 MW;  FAF26BA2F8A9A923 CRC64;
     MQQTTSPLNL SNLVNRNAHF IGGAWEPSTS GAIDVINPAN GEVVGRVPNG GAAQAAKAIE
     AAHRAQREWA ARTPAQRAVF MHAWAARIRD NADHLARILT SEQGKPLSES LEEAEGVAMF
     IEWYAEEGKR AYGETIPALA RNKRILVIPQ PVGVTALITP WNYPGTMIAR KGAPALAAGC
     TVVLKPASQT PLTAVALVAL AQEAGFPAGV INLVTGKASE IGEEFMTNAQ VRKVSFTGST
     EVGKLLIRAS AEQVKRLSLE LGGNAPFIVF PDADLDAAVA AAVGNKFENC GQMCNGINVM
     YVHEDIAQRF SRMVAQKVAS LKVGNGLEEG VQLGPVIDHR AVAFVDKLVQ EAVQQGAKVE
     VGGSCLTATP YQKGSFYSPT VLTGVTTEMR IAQEEVFGPV APIVTFSSEE EVLALANATP
     FGLAAYVFTK DVRRVFEVSE QLEFGMVGVN SASLSVPQAP FGGIKQSGQG REGGHHGLEE
     FMEIKYISLT L
//
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