ID H6RJM7_BLASD Unreviewed; 486 AA.
AC H6RJM7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative NAD+-dependent aldehyde dehydrogenase {ECO:0000313|EMBL:CCG02332.1};
GN OrderedLocusNames=BLASA_1397 {ECO:0000313|EMBL:CCG02332.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG02332.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG02332.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG02332.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; FO117623; CCG02332.1; -; Genomic_DNA.
DR RefSeq; WP_014375229.1; NC_016943.1.
DR AlphaFoldDB; H6RJM7; -.
DR STRING; 1146883.BLASA_1397; -.
DR KEGG; bsd:BLASA_1397; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_11; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000007517; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT DOMAIN 20..477
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 9..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 486 AA; 51555 MW; 36C7CAEFFB95FD04 CRC64;
MTALIDNLVD GTWSQNGDGS PQPNLNPADQ RDVVGVYPMA TEAQAAEVVD AAVKAFPGWR
RTSAIDRGVF LSRAADLLRE RSESIAADIT RENGKTLAEA RVEVIKSADF LDYYAGIARL
PFGDLLDDAR PNAFVLTRRE PIGVIVAITP WNDPLLTPAR KISPALVTGN TVVVKPSPET
PLSMQHLARA LHDAGLPAGV LNTVNAANEV VGSAVLADDR IAAVTFTGST RTGFALQRAL
AGRTVRFQAE MGGKNASVVM PDADLDLAVK TIAAAAFAQA GQRCTATSRV IAHSDVHDLL
VERLVSAAAT YRPGDGARGA VMGPVVHRDH QASVLRFVHE AQSQGATVLT GGDAPTDDDR
KHGCFVNPTV LGDVTPEMTI WRQEVFGPVI AVVRAADLDH AVALVNESDY GLSAAIFTAD
LHAAHRFIDE VDTGQVSVNL PTSGWDVHQP FGGFKQSGSS FKEQGLDALR YYTKTKTAAI
AHGVLP
//
