ID A0A0G3IGK8_9MYCO Unreviewed; 488 AA.
AC A0A0G3IGK8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AKK26668.1};
GN ORFNames=AB431_08160 {ECO:0000313|EMBL:AKK26668.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK26668.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK26668.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK26668.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
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; CP011773; AKK26668.1; -; Genomic_DNA.
DR RefSeq; WP_047329509.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IGK8; -.
DR STRING; 1545728.AB431_08160; -.
DR KEGG; mye:AB431_08160; -.
DR PATRIC; fig|1545728.4.peg.1657; -.
DR OrthoDB; 9761688at2; -.
DR Proteomes; UP000035237; 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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 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 15..481
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 488 AA; 51539 MW; 7D2A51ECB86DA01D CRC64;
MAVVSEQRTY VAGRWVTGDE LISVENPADE THVHDVTATP IREVERAITE ARGSFDRGVW
ADLAVADRAR VLRDFVDFIE SSADTLVPTL VAEAGQSRRF AEMTQLQAGL NLARQTINLY
LSMKHEQASP VPVDDLVRGR VALSIRRHEP VGVVTAITPY NAALIMGFQK LIPALMAGNS
VILRPSPLTP ISSLIFGMAA EAVGLPPGVL SVVAEQGTAG AELLTSHGCV DMVSFTGSTL
AGRKILAQAA PTVKRVSLEL GGKSAQIYLA DAIERVAAGA AMVVMSTAGQ ACVAATRMLV
PEDQRERVLE TVGAVYKSIK VGPPSSPDAT MGPVISAAQR ERCERLVAAA EEHGGKVVCG
GGRPPGLDRG YYVEPTVLDI PDNANPAAQE EIFGPVIAVL GYRDLDHAVE IANDSIYGLS
GQVYGADVAA ALSVARRLRT GAVNVNTTVF SAYAPSGGYK QSGLGRERGP DGIREFQEVK
HLSIGELS
//
