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Database: UniProt/TrEMBL
Entry: G8XED8_STREN
LinkDB: G8XED8_STREN
Original site: G8XED8_STREN 
ID   G8XED8_STREN            Unreviewed;       445 AA.
AC   G8XED8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   OrderedLocusNames=SCATT_p10990 {ECO:0000313|EMBL:AEW99292.1};
OS   Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS   / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OG   Plasmid pSCATT {ECO:0000313|EMBL:AEW99292.1,
OG   ECO:0000313|Proteomes:UP000007842}.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptantibioticus.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW99292.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RC   PLASMID=Plasmid pSCATT {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-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; CP003229; AEW99292.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8XED8; -.
DR   KEGG; scy:SCATT_p10990; -.
DR   PATRIC; fig|1003195.29.peg.6894; -.
DR   HOGENOM; CLU_005391_3_1_11; -.
DR   OMA; RHGKRWM; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000007842; Plasmid pSCATT.
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; cd07087; ALDH_F3-13-14_CALDH-like; 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}; Plasmid {ECO:0000313|EMBL:AEW99292.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007842}.
FT   DOMAIN          16..439
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   445 AA;  47155 MW;  B7A78110DB293405 CRC64;
     MVSTVSTTPA PAETPADVVA RLRATFRTGR TRPLAWRTEQ LRRLRRMLTE EGAELIAALH
     ADLGKSEAEA RRTEIDFTVR EIDHTLDHLD QWLAPRPAPV PAFLGDATAW TVLDPLGVVL
     VIAPWNYPAQ LLLAPVVGAL ASGNCVVAKP SELAPATSAA LARLLPRHLD TDAVAVVEGG
     VPETTALLEQ RFDHILYTGN ATVGRVVMTA AARHLTPVTL ELGGKSPAFV DAGTDPAVVA
     ARLAAGKFLN AGQTCVAPDY VLTDPGTARA LEAALADAVR GLYGPDPAAS PEYGRIVNER
     HFDRLTALLG SGRTVVGGEH DRATRYIAPT VLAEVPADAP VMREEIFGPI LPIVEVAGVD
     EAIAFINGRE KPLALYAFTD SAEVRRRLTA ETSSGGLGFG LPVAHLTVPD LPFGGVGESG
     MGRYHGHWSI ETFSHRKAVL GKPLG
//
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