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Database: UniProt/TrEMBL
Entry: Q0S3M8_RHOJR
LinkDB: Q0S3M8_RHOJR
Original site: Q0S3M8_RHOJR 
ID   Q0S3M8_RHOJR            Unreviewed;       507 AA.
AC   Q0S3M8;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:ABG97858.1};
DE            EC=1.2.1.- {ECO:0000313|EMBL:ABG97858.1};
GN   OrderedLocusNames=RHA1_ro06081 {ECO:0000313|EMBL:ABG97858.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97858.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000431; ABG97858.1; -; Genomic_DNA.
DR   RefSeq; WP_009479319.1; NC_008268.1.
DR   AlphaFoldDB; Q0S3M8; -.
DR   KEGG; rha:RHA1_ro06081; -.
DR   PATRIC; fig|101510.16.peg.6132; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_11; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000008710; 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   CDD; cd07116; ALDH_ACDHII-AcoD; 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   PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          28..494
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   507 AA;  55107 MW;  3C539817B9F64F31 CRC64;
     MTVYARPGSP DAVMSFQSRY DNWIGGQWVA PVKGQYFENP TPVTGQPFCE VARSTSEDIE
     LALDAAHAAA PAWGKTSVAE RAIILNKIAD RIEENLESIA LAESWDNGKP IRETLNADIP
     LAVDHFRYFA GAIRAQEGAL SEIDSDTVAY HFHEPLGVVG QIIPWNFPIL MAVWKLAPAL
     AAGNAVVLKP AEQTPASILH LISVIGDLLP AGVVNIVNGF GVEAGKPLAS SPRIRKIAFT
     GETTTGRLIM QYASQNLIPV TLELGGKSPN IFFSDVLSSN DDYQDKALEG FTMFALNQGE
     VCTCPSRSLI QEDIFDEFLA MAAIRTKAVR QGDPLDTDTM IGAQASNDQL EKILSYIEIG
     KGEGAKVVTG GERAELGGDL SGGYYVQPTI FTGQNKMRIF QEEIFGPVVS VTSFKDYDQA
     IEIANDTLYG LGAGVWSRDG GVAYRAGRDI QAGRVWTNTY HQYPAHAAFG GYKQSGIGRE
     NHLMMLEHYQ QTKNLLVSYA QKAQGFF
//
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