ID S2XAF7_9STAP Unreviewed; 495 AA.
AC S2XAF7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=HMPREF1208_01966 {ECO:0000313|EMBL:EPD48651.1};
OS Staphylococcus sp. HGB0015.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1078083 {ECO:0000313|EMBL:EPD48651.1, ECO:0000313|Proteomes:UP000014407};
RN [1] {ECO:0000313|EMBL:EPD48651.1, ECO:0000313|Proteomes:UP000014407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0015 {ECO:0000313|EMBL:EPD48651.1,
RC ECO:0000313|Proteomes:UP000014407};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Staphylococcus sp. HGB0015.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPD48651.1}.
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DR EMBL; AGEO01000023; EPD48651.1; -; Genomic_DNA.
DR RefSeq; WP_016426180.1; NZ_KE150418.1.
DR AlphaFoldDB; S2XAF7; -.
DR GeneID; 64048433; -.
DR PATRIC; fig|1078083.3.peg.1944; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_9; -.
DR Proteomes; UP000014407; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 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; 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|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000014407}.
FT DOMAIN 21..483
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 495 AA; 53801 MW; 5E48205AB4A0EE1F CRC64;
MGINVKDYVS DQYELFIGGE FVKPESGEYL DVSNPATGEV LAKVAKANEQ DVDKAVKAAQ
DAFPEWSRKS KQERSNLLRQ IHDKLMEKKD HFATIETLNT GKAIRESANI DIPSAARHYQ
YFASVVDTDE GSLNNIEDNV MSIIQHEPIG VVGAVVAWNF PMLLASWKLG PALAAGNTVV
IQPSSSTPLS LIELAKIFQE VLPAGVVNVV TGKGSESGNA IFNHEGVDKL SFTGSTDVGY
QVAEAGAKRI VPATLELGGK SANIILDDAN LDLALEGIQL GILFNQGEVC SAGSRLLVHE
KIYDTLVPRL VEAFKQIRVG DPLDSATQMG SQTGQAQIDK IQGYIDYAKE NDANILVGGH
RLTDNGLDKG HFFEPTLIEV KDNKNKLAQE EIFGPVLTII KVKDDEEAIQ IANDSEYGLA
GGVFSTNINR ALNVAKNVRT GRVWVNTYNQ VPEGAPFGGY KKSGIGRETY KDAIANYQQV
KNIYIDISNE TKGLY
//
