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Database: UniProt/TrEMBL
Entry: Q217B5_RHOPB
LinkDB: Q217B5_RHOPB
Original site: Q217B5_RHOPB 
ID   Q217B5_RHOPB            Unreviewed;       506 AA.
AC   Q217B5;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Aldehyde dehydrogenase (NAD+) {ECO:0000313|EMBL:ABD87521.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:ABD87521.1};
GN   OrderedLocusNames=RPC_1964 {ECO:0000313|EMBL:ABD87521.1};
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD87521.1};
RN   [1] {ECO:0000313|EMBL:ABD87521.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18 {ECO:0000313|EMBL:ABD87521.1};
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., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   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; ABD87521.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q217B5; -.
DR   STRING; 316056.RPC_1964; -.
DR   KEGG; rpc:RPC_1964; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_5; -.
DR   OrthoDB; 8175464at2; -.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          32..493
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   506 AA;  55209 MW;  6E9F334D0AAA23B2 CRC64;
     MKYAAPGTAG APVDFKSRYD NFIGGRWSAP VNGRYFDSVT PITGQAFTQA ARSDEVDITL
     ALDAAHAAAD AWGRTSVAER ALVLNRIADR MEENLERLAY AESVDNGKPI RETLAADIPL
     AIDHFRYFAS CVRSQEGTLA QLDEHTVAYH FHEPLGVVGQ IIPWNFSILM AAWKLAPALA
     SGNCIVLKPA EQTPISILVL VELIADLLPP GVLNVVNGFG LEAGKPLASS NRISKIAFTG
     ETSTGRLIMQ YASANLIPVS LELGGKSPNI FFDDVAASDD AYFDKAIEGF VMFALNQGEV
     CTCPSRALIQ ESLYDRFIDR ALARVTAIRQ GNPLDTETMI GAQASSEQME KILSYFTIGR
     DEGAKVLTGG ARAELGGDLA EGYYVQPTVL KGHNRMRVFQ EEIFGPVVAV TTFKDEDEAL
     HLANDTHYGL GAGVWTRDGN RAYRFGRGIK AGRVWTNCYH LYPAHAAFGG YKQSGIGREN
     HHMMLDHYQQ TKNLLVSYSP DALGFF
//
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