ID K0IZM4_AMPXN Unreviewed; 452 AA.
AC K0IZM4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN Name=aldH {ECO:0000313|EMBL:BAM46417.1};
GN OrderedLocusNames=AXY_02850 {ECO:0000313|EMBL:BAM46417.1};
OS Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS / NBRC 15112 / Ep01).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM46417.1, ECO:0000313|Proteomes:UP000006294};
RN [1] {ECO:0000313|EMBL:BAM46417.1, ECO:0000313|Proteomes:UP000006294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC Ep01 {ECO:0000313|Proteomes:UP000006294};
RA Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; AP012050; BAM46417.1; -; Genomic_DNA.
DR RefSeq; WP_015009023.1; NC_018704.1.
DR AlphaFoldDB; K0IZM4; -.
DR STRING; 698758.AXY_02850; -.
DR KEGG; axl:AXY_02850; -.
DR PATRIC; fig|698758.3.peg.287; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_3_1_9; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000006294; 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 GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07136; ALDH_YwdH-P39616; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 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|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000006294}.
FT DOMAIN 18..424
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 206
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 240
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 452 AA; 51264 MW; 7ABE17EAF820CC86 CRC64;
MDLLERQKDF FYSGVTRPYQ YRKRALTLLK GTIKNNESKI MKALQRDLNK SDFEAFTTEI
GLVYTEIDFV LKHLKKWMKP KRVKTPMTHV GSVSRIYPDP FGVALIISPW NYPFQLAMTP
LVGAIAGGNT AVIKPSELTP TVSKLIKEII DQTFIEDYIA VELGGVETSQ KLLDQAFDYI
FFTGSVPVGK IVMEKASQNL TPITLELGGK SPVIVHDDAS LKLAAKRIAW GKFTNAGQTC
VAPDYLFVQE NVKEQFLTYL KEAIIHLYGE RPLDNPDYGK IVSDKHFQRL VGYLNNGEVC
YGGTVDEEKH KIEPTILTDV DRHQAIMHEE IFGPILPVLT YSHLDEAIDY IRRQPKPLSF
YLFSETAHIQ NTVLEQISFG GGCINDTLYH LGSPHLPFGG IGESGIGSYR GKFSFETFTH
QKSVLKQSSR LDLPFRYPNK KNRMKWARRV MK
//
