ID A4TEK1_MYCGI Unreviewed; 507 AA.
AC A4TEK1;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Aldehyde dehydrogenase (NAD(+)) {ECO:0000313|EMBL:ABP47418.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:ABP47418.1};
GN OrderedLocusNames=Mflv_4952 {ECO:0000313|EMBL:ABP47418.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP47418.1};
RN [1] {ECO:0000313|EMBL:ABP47418.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47418.1};
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., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP47418.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47418.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000656; ABP47418.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TEK1; -.
DR STRING; 350054.Mflv_4952; -.
DR KEGG; mgi:Mflv_4952; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_11; -.
DR OrthoDB; 6882680at2; -.
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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 28..494
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 507 AA; 54862 MW; 184DB953F88BE7DA CRC64;
MTVYARPGAD GSLMSFKPRY DNFIGGQWVA PTAGRYFENP SPVTGQPFTE VARSDEADIE
KALDAAHAAA PAWGKTSAAE RAVILNKIAD RIEENLESIA LAESWDNGKP IRETLNADLP
LAVDHFRYFA GCIRAQEGSL SEVDADTVAY HFHEPLGVVG QIIPWNFPIL MAVWKLAPAL
AAGNAVVLKP AEQTPASILY LMEVIGDLLP AGVVNVVNGF GVEAGKPLAS SNRIAKIAFT
GETTTGRLIM QYASQNLIPV TLELGGKSPN IFFNDVLAAS DDYQDKALEG FTMFALNQGE
VCTCPSRSLI QADIYDEFLA LAAIRTKAVR QGDPLDTETM IGAQASNDQL EKILSYIEIG
KSEGAKVVTG GERAELGGDL NGGYYVAPTI FTGNNTMRIF QEEIFGPVVA VTSFTDYDDA
ISLANDTLYG LGAGVWSRNG NTAYRAGRDI KAGRVWTNCY HQYPAHAAFG GYKQSGIGRE
NHRMMLDHYQ QTKNLLVSYS DQALGFF
//
