ID C1B515_RHOOB Unreviewed; 491 AA.
AC C1B515;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:BAH50941.1};
DE EC=1.2.1.- {ECO:0000313|EMBL:BAH50941.1};
GN OrderedLocusNames=ROP_26940 {ECO:0000313|EMBL:BAH50941.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH50941.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH50941.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH50941.1,
RC ECO:0000313|Proteomes:UP000002212};
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 erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011115; BAH50941.1; -; Genomic_DNA.
DR RefSeq; WP_012689897.1; NC_012522.1.
DR AlphaFoldDB; C1B515; -.
DR STRING; 632772.ROP_26940; -.
DR KEGG; rop:ROP_26940; -.
DR PATRIC; fig|632772.20.peg.2817; -.
DR HOGENOM; CLU_005391_1_0_11; -.
DR OMA; WINSHFQ; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000002212; 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 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; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-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}.
FT DOMAIN 35..487
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 491 AA; 51039 MW; CD66DC3FB08BE693 CRC64;
MTTTVTEPTG SHIRNEVPTA QHLVNGEWLG EADTARWNPA RPNELAAYSP SGGTAEVDAA
VAAAAAAQPA WAALPAPARG AILIKAANLL QERGSAVAAD LVREEGKTLA EARGEVTRAV
DVLRFFGSLG WAATGEVLPS GLPGTSITTR REPLGVFALI TPWNFPIAIP AWKTAPALIS
GNTVVLKPAE LTPLSATHLA RALQDAGLPA GVFNVVHGKG RVVGDALARD PRVAGLSFTG
STTVGLGLQD ILNSRRARVQ LEMGGKNAVL VLDDARNAAQ VVAAGAFGLT GQACTATSRV
YVTPGIRDAF LEALVEEAAR YVPGDGSADT TRMGAVVSRA QFEQDQEAVR SAVLRGATLR
HGDYAGDTSA GFFFPATVLT DLPLDDPAVT DEIFGPVVAV LEVADYEAGL AAVNDSRYGL
TAGICTDSLT RSTDFAARAQ AGVVKINRPT AGLDLNVPFG GVKDSSTNTF REQGRSAVDF
YTWGKTVYTG V
//