ID A0A0M2H3T5_9MICO Unreviewed; 509 AA.
AC A0A0M2H3T5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Putative aldehyde dehydrogenase AldA {ECO:0000313|EMBL:KJL39061.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:KJL39061.1};
GN Name=aldA {ECO:0000313|EMBL:KJL39061.1};
GN ORFNames=RS81_02155 {ECO:0000313|EMBL:KJL39061.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL39061.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL39061.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL39061.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL39061.1}.
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DR EMBL; JYIZ01000052; KJL39061.1; -; Genomic_DNA.
DR RefSeq; WP_045276092.1; NZ_JYIZ01000052.1.
DR AlphaFoldDB; A0A0M2H3T5; -.
DR STRING; 92835.RS81_02155; -.
DR PATRIC; fig|92835.4.peg.2187; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000033956; Unassembled WGS sequence.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT DOMAIN 36..476
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 476..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 509 AA; 54321 MW; D16E4D513169489E CRC64;
MSFLEYAPAP ESRGILNLRD DYGLFINGGF RAGGGSPFAT ISPADEQHIA TIASASDDDV
DAAVAAARRA YERTWSKMSG RDRGKYLFRI ARLVQERARE LAVAESLDNG KPIKESRDVD
VPLVAAWFFY YAGWADKLDY AGLGPDPQAL GVAAQVIPWN FPLLMLAWKV APALAAGNTV
VLKPAETTPL TALLFAEILQ QADLPPGVVN IITGAGATGA ALVRHPDVDK VAFTGSTAVG
REIAKAVAGT GKKVTLELGG KAANIIFDDA PIDQAVDGIV TGIFFNQGQV CCAGSRLVVQ
ESIHDEVVDR LKRRLSTLRL GDPLDKNTDI GAINSAEQLA RVRELSRIGE EEGAERWTAD
CPIPDRGFWF APTIFTGVQA SHRIARDEIF GPVLSVLTFR TPAEAIAKAN NTPYGLSAGI
WTEKGSRILA VADKLRAGVV WANTFNRFDP SSPFGGYKES GYGREGGKHG LAAYLKGASS
PSRSRALSDG GGTRRAATKR AESKKGIRA
//
