ID A0A2A9DX84_9MICO Unreviewed; 503 AA.
AC A0A2A9DX84;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Acyl-CoA reductase-like NAD-dependent aldehyde dehydrogenase {ECO:0000313|EMBL:PFG30986.1};
GN ORFNames=ATJ78_1931 {ECO:0000313|EMBL:PFG30986.1};
OS Microbacterium agarici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=630514 {ECO:0000313|EMBL:PFG30986.1, ECO:0000313|Proteomes:UP000221369};
RN [1] {ECO:0000313|EMBL:PFG30986.1, ECO:0000313|Proteomes:UP000221369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21798 {ECO:0000313|EMBL:PFG30986.1,
RC ECO:0000313|Proteomes:UP000221369};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG30986.1}.
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DR EMBL; PDJE01000001; PFG30986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9DX84; -.
DR Proteomes; UP000221369; Unassembled WGS sequence.
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; 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; 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:UP000221369}.
FT DOMAIN 30..475
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 480..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 503 AA; 53384 MW; D540C10589300838 CRC64;
MSFLEYAPAP ESTAILNLKD EYGLFIGGEF VEGSGQPFQT ISPADESTIA TVQTADASDV
DRAVAAARTA YDRVWSKMSG ADRGKYLFRI ARLVQERARE LAVAESLDNG KPIKESRDVD
VPLVAAWFFY YAGWADKLDY AGLGPNPRSL GVAGQVIPWN FPLLMLSWKI APALAAGNTV
VLKPAETTPL TALLFAEIVQ QAGLPAGVVN IITGAGATGQ SLVQHPDVNK VAFTGSTGVG
RAIAKSVAGT DKKLTLELGG KAANIVFDDA PIDQAIEGIV NGIFFNQGHV CCAGSRLLVQ
ESIHDEVIER LKSRLSTLRL GDPLDKNTDI GAINSSEQLA RITALADAGE AEGAERWTAP
CELPAHGYWF APTIFTGVST SHRIARDEIF GPVLSVLTFR TPAEAIAKAN NTPYGLSAGI
WTDKGSRILA VADKLRAGVI WANTFNRFDP ASPFGGYKES GYGREGGRHG LGAYLAPAGA
PAAALPQKKS RSLTRTSTKE NGK
//