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Database: UniProt/TrEMBL
Entry: Q212F1_RHOPB
LinkDB: Q212F1_RHOPB
Original site: Q212F1_RHOPB 
ID   Q212F1_RHOPB            Unreviewed;       476 AA.
AC   Q212F1;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   29-OCT-2014, entry version 57.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:ABD88735.1};
GN   OrderedLocusNames=RPC_3193 {ECO:0000313|EMBL:ABD88735.1};
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88735.1, ECO:0000313|Proteomes:UP000001948};
RN   [1] {ECO:0000313|EMBL:ABD88735.1, ECO:0000313|Proteomes:UP000001948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18 {ECO:0000313|EMBL:ABD88735.1,
RC   ECO:0000313|Proteomes:UP000001948};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000301; ABD88735.1; -; Genomic_DNA.
DR   RefSeq; WP_011473624.1; NC_007925.1.
DR   RefSeq; YP_533054.1; NC_007925.1.
DR   ProteinModelPortal; Q212F1; -.
DR   STRING; 316056.RPC_3193; -.
DR   EnsemblBacteria; ABD88735; ABD88735; RPC_3193.
DR   GeneID; 3972204; -.
DR   KEGG; rpc:RPC_3193; -.
DR   PATRIC; 23271182; VBIRhoPal29154_3276.
DR   eggNOG; COG1012; -.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00128; -.
DR   OMA; RNSQAPC; -.
DR   OrthoDB; EOG6BS8QW; -.
DR   BioCyc; RPAL316056:GH3E-3233-MONOMER; -.
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; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001948};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003344};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001948}.
SQ   SEQUENCE   476 AA;  50235 MW;  6896551003B6817C CRC64;
     MVNRMQFYID GAWVDPVVKK STPVVNPATE EAMYEVALGS KADVDNAVAA AKRAFETFSQ
     TSREQRVALL EKIIAVYKTR MKDIGAAVSD EMGAPLPFAE KFQAGAGLGH IASTLEVLKT
     YNFEEPLGNA VVVREPVGVI GMITPWNWPL NQIACKVAPA LAAGCTMILK PSEFTPSSAL
     IFAEILHEAG VPNGVFNLVN GLGPEVGAAM SEHPDIDMIS FTGSTRAGID VAKRAAPTVK
     RVSQELGGKS PNIILEDADL QKAVAGGVAH MFNNSGQSCN APSRMIVPQS KMKEVAAIAK
     AVADKTKAGD PRAEGTSIGP VVSRIQWDKI QALIQKGVEE GATLVAGGPG LPEGVNKGFY
     VRPTVFADVT NDMTIAREEI FGPVIAIIGA KDEADAVKIA NDTPYGLAGY VSAGSVERAR
     AVGRKLRAGN VNLNGVPNER TAPFGGYKQS GNGREWGKFG LEEYLEVKAI AGYNAA
//
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