(data stored in ACNUC1104 zone)

SWISSPROT: C0ZLB0_RHOE4

ID   C0ZLB0_RHOE4            Unreviewed;       517 AA.
AC   C0ZLB0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   SubName: Full=Putative aldehyde dehydrogenase {ECO:0000313|EMBL:BAH30800.1};
DE            EC=1.2.1.- {ECO:0000313|EMBL:BAH30800.1};
GN   OrderedLocusNames=RER_00920 {ECO:0000313|EMBL:BAH30800.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH30800.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH30800.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AP008957; BAH30800.1; -; Genomic_DNA.
DR   RefSeq; WP_003943578.1; NC_012490.1.
DR   STRING; 234621.RER_00920; -.
DR   EnsemblBacteria; BAH30800; BAH30800; RER_00920.
DR   GeneID; 31539966; -.
DR   KEGG; rer:RER_00920; -.
DR   PATRIC; fig|234621.6.peg.521; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271512; -.
DR   KO; K00135; -.
DR   OMA; NWNKQLT; -.
DR   BioCyc; RERY234621:GHDE-95-MONOMER; -.
DR   Proteomes; UP000002204; 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   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0ZLB0.
DR   SWISS-2DPAGE; C0ZLB0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000313|EMBL:BAH30800.1}.
FT   DOMAIN       29    481       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    254    254       {ECO:0000256|PROSITE-ProRule:PRU10007}.
SQ   SEQUENCE   517 AA;  54842 MW;  39D70111C0836478 CRC64;
     MPAPSAATFS RLADLIAIDN VADRPTKSIT EVFTGKELAT IPVGTADDAL AAIARARVAQ
     KEWAKRSVLD RAAVFHRYRD LILENRDALM DMAQAETGKS RTAAQEEVLD ISMTSRHYAR
     VAPKLLRPRR VSGMLPGLTK TVVRYQPKGV VGVISPWNYP MTLAVSDAIA ALLAGNAVVL
     KPDSQTPYCA LACVELLYKA GLPRDLFAVV PGPGSVVGTA LVENTDYLMF TGSTATGQLL
     AEQAGRRLIG FSAELGGKNP MIVAAGADLR EVTDAAVRAC FSNSGQLCIS IERIYVEESI
     APEFIRMFGD RVKKMNLAAG YEFGIEMGSL VSEAQVKAIS AHVDDAVVKG ATVIAGGKAR
     PDIGPLFYEP TLLTGVPEDA ECYRDETFGP LVSIYPVKDV EEAIAAANDT EYGLNASVWA
     GSKAAGEAIA ARIHAGTVNV DEGYAPTWGS TAAPMGGMGV SGVGRRHGAE GLIKYTEPQT
     VATTRVMNLG GPRGLPAKVW AKLMPHAIKI MSWVPGR
//

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