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Database: UniProt/TrEMBL
Entry: F8IJI4_ALIAT
LinkDB: F8IJI4_ALIAT
Original site: F8IJI4_ALIAT 
ID   F8IJI4_ALIAT            Unreviewed;       497 AA.
AC   F8IJI4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:AEJ44697.1};
GN   OrderedLocusNames=TC41_2804 {ECO:0000313|EMBL:AEJ44697.1};
OS   Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ44697.1, ECO:0000313|Proteomes:UP000000292};
RN   [1] {ECO:0000313|EMBL:AEJ44697.1, ECO:0000313|Proteomes:UP000000292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ44697.1,
RC   ECO:0000313|Proteomes:UP000000292};
RX   PubMed=21914900; DOI=10.1128/JB.05709-11;
RA   Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT   "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT   4-1.";
RL   J. Bacteriol. 193:5602-5603(2011).
RN   [2] {ECO:0000313|Proteomes:UP000000292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA   Chen Y., He Y., Dong Z., Hu S.;
RT   "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT   1.";
RL   Submitted (JUN-2011) 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; CP002902; AEJ44697.1; -; Genomic_DNA.
DR   RefSeq; WP_014465523.1; NC_017167.1.
DR   AlphaFoldDB; F8IJI4; -.
DR   STRING; 1048834.TC41_2804; -.
DR   KEGG; aad:TC41_2804; -.
DR   PATRIC; fig|1048834.4.peg.2662; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_5_1_9; -.
DR   OMA; VRHVMIK; -.
DR   OrthoDB; 9758906at2; -.
DR   Proteomes; UP000000292; Chromosome.
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; cd07091; ALDH_F1-2_Ald2-like; 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; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 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}.
FT   DOMAIN          33..492
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   497 AA;  53866 MW;  E2D42DCFA7CD4A57 CRC64;
     MAVQEVNASA LHPDVVEFLT GPKGLFIDGE FVPSLSGKTF KSINPATEEV LVEVAEAEAP
     DIDRAVKAAR RAFESGPWSR MSAAERSRLL YRLADLMEEH KLQLAQLETL DNGKPIRESL
     NADLPLAIEH IRYYAGWPTK VVGQTIPVAG KYFNYTRHEP VGVVGQIIPW NFPLLMACWK
     IGAALAMGCT VVLKPAEQTP LSALYLAKLI QEAGFPPGVV NVVPGFGETA GQALVEHPDV
     NKIAFTGSTE VGKLIMRNAA ATLKRVTLEL GGKSPNIILP DADMSRAIPG AFMGIMFNQG
     QVCCAGSRLF VQKKAYDNVV ADLVSLAKKI RQGPGLDQST EMGPLVSDEQ EKRVLGYIEK
     GVEEGAEVLV GGGKATDRGY FVQPTIFANV RDDMTIAREE IFGPVVAAMP FEDLDEVIAR
     ANDTEYGLAA GVWTENIRNA HYIASKLKAG TVWVNCYNVF DAAAPFGGYK QSGIGREMGS
     YALNNYTEVK DVWISLS
//
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