ID B9DIL6_STACT Unreviewed; 479 AA.
AC B9DIL6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN Name=gabD {ECO:0000313|EMBL:CAL29266.1};
GN OrderedLocusNames=Sca_2363 {ECO:0000313|EMBL:CAL29266.1};
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL29266.1, ECO:0000313|Proteomes:UP000000444};
RN [1] {ECO:0000313|EMBL:CAL29266.1, ECO:0000313|Proteomes:UP000000444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300 {ECO:0000313|EMBL:CAL29266.1,
RC ECO:0000313|Proteomes:UP000000444};
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL29266.1; -; Genomic_DNA.
DR RefSeq; WP_015901601.1; NC_012121.1.
DR AlphaFoldDB; B9DIL6; -.
DR GeneID; 60543935; -.
DR KEGG; sca:SCA_2363; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_5_1_9; -.
DR OrthoDB; 9762913at2; -.
DR BioCyc; SCAR396513:SCA_RS11885-MONOMER; -.
DR Proteomes; UP000000444; 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; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036492}.
FT DOMAIN 18..473
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 479 AA; 51308 MW; 04E0983CBA672E17 CRC64;
MVDNLNHNWI NGKKVQTDNT LKVTNPATNE VIGEVPSVTE GLINDAIDAS YQAFSSWSKL
TAAERAEYLH AWADNLLQKK EKLASIMTEE QGKPYGESLG EIEGCAQFIK WNAEEGKRIY
GEIIPPSSPN QRISVIKQPV GVCALITPWN FPGAMVARKV SPALAAGCTV IVKPSSETPR
IAIAILDELM ATGIDNGAAN LITGKSSLIS ETLLNDRRVS KISFTGSTDI GKLLMKKAAD
QVKRISLELG GNAPVIVLND ADLDKAADAI VENKFENTGQ MCNGINTVLA QSEVKDELIT
KVIERVTQLR VGPGNQKDVQ VGPLINSGAI EKVEKLVSEA EKAGANIATG GKKVENSPSD
LFYQPTVVTN VKPEMSIAKE EIFGPVAPII SFDTIAEAIK IANASPYGLA AYFFSNNVNT
VYQVSEQLDF GMIGVNGTQL SVPQAPFGGI KESGMGREGG HYGLDGFLEL KYISLSLDA
//
