ID Q5HN16_STAEQ Unreviewed; 459 AA.
AC Q5HN16;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN Name=aldA-1 {ECO:0000313|EMBL:AAW54852.1};
GN OrderedLocusNames=SERP1456 {ECO:0000313|EMBL:AAW54852.1};
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW54852.1, ECO:0000313|Proteomes:UP000000531};
RN [1] {ECO:0000313|EMBL:AAW54852.1, ECO:0000313|Proteomes:UP000000531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531};
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J., Khouri H., Utterback T., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K., Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54852.1; -; Genomic_DNA.
DR RefSeq; WP_002494628.1; NC_002976.3.
DR AlphaFoldDB; Q5HN16; -.
DR STRING; 176279.SERP1456; -.
DR KEGG; ser:SERP1456; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_3_1_9; -.
DR Proteomes; UP000000531; 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 Coiled coil {ECO:0000256|SAM:Coils}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000000531}.
FT DOMAIN 9..429
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT COILED 23..50
FT /evidence="ECO:0000256|SAM:Coils"
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 459 AA; 51987 MW; A968A0B2E49DABED CRC64;
MTIIRDKFNN SKAFFNTHKT KNLKFRKQQL KLLSKNIKNH ENELLDALYK DLGKSKVEAY
ATEISMLLKS IKLMRKELKN WSKTKQTDTP LYLFPTKSYI KKEPYGTVLI IGPFNYPVQL
VFEPLIGAIA AGNTAIVKPS ELTPHVAIVI KDIIEDTFDE AYVSVVEGGI EETQALLSLP
FDYMFFTGSE KVGKIVYEAA ARKLIPVTLE LGGKSPVIVD DTANIKVASE RISFGKFTNA
GQTCVAPDYI LVQRKVKNDL IKALKKTIIE FYGENIEKSP DFGRIVNQKH FNRLNDLIQI
HKDNVVFGGN SSKEDLYIEP TLLDNITNDN KIMKEEIFGP ILPIITYDNF DEVLEIIQSK
SKPLSLYLFS EDENMTHRVV EELSFGGGAI NDTLMHLANP NLPFGGVGSS GIGQYHGKYS
FDTFSHMKSY TFKSTRLESS LFFPPYKGKF KYIKTFFKN
//
