ID A7Z7P2_BACVZ Unreviewed; 456 AA.
AC A7Z7P2;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN OrderedLocusNames=RBAM_026600 {ECO:0000313|EMBL:ABS75018.1};
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423 {ECO:0000313|EMBL:ABS75018.1, ECO:0000313|Proteomes:UP000001120};
RN [1] {ECO:0000313|EMBL:ABS75018.1, ECO:0000313|Proteomes:UP000001120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / FZB42
RC {ECO:0000313|Proteomes:UP000001120};
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Sussmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS75018.1; -; Genomic_DNA.
DR RefSeq; WP_012118189.1; NC_009725.2.
DR AlphaFoldDB; A7Z7P2; -.
DR KEGG; bay:RBAM_026600; -.
DR HOGENOM; CLU_005391_3_1_9; -.
DR Proteomes; UP000001120; 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}.
FT DOMAIN 7..428
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 210
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 244
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 456 AA; 50533 MW; 5C12A407C631B74F CRC64;
MNSIPSIVSK HKAYFAAGHT RQLESRLNML QKLKQAIKTQ EADITAALYQ DLHKSEQESY
TTEIGIVLEE ISFVMKRLGK WVKPKRVKTP LTHLGSKSII IPEPYGTVLV IAPWNYPLQL
ALSPLIGAIA AGNTVVLKPS EYTPAVSAVL SKLISSVFPS DYVAMAEGGP DVSTVLLQQP
FDYIFFTGSV AVGKIVMEAA AKQLIPVTLE LGGKSPCIVH KDADIQLAAK RIVFGKFTNA
GQTCIAPDYL FVHQDIKTKL TEEMKRAISE FYGPQPEQNP QYGKIVSERH YQRLLSFLND
GIPLTGGQFN PDHHKIAPTI LDQVKDDSPV MQEEIFGPIL PLFTYGDIDE VIEKVQSRPK
PLALYLFTTN KETERAVLEN LSFGGGCVND TLMHVATPYL PFGGVGESGI GSYHGFDSFN
TFTHKKSVVK QTNRFDFAFR YPSSKNGLRM IRKILK
//
