ID A0A1Y5T8T3_9RHOB Unreviewed; 772 AA.
AC A0A1Y5T8T3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Putative aldehyde dehydrogenase AldA {ECO:0000313|EMBL:SLN56379.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:SLN56379.1};
GN Name=aldA {ECO:0000313|EMBL:SLN56379.1};
GN ORFNames=PSJ8397_02990 {ECO:0000313|EMBL:SLN56379.1};
OS Pseudooctadecabacter jejudonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooctadecabacter.
OX NCBI_TaxID=1391910 {ECO:0000313|EMBL:SLN56379.1, ECO:0000313|Proteomes:UP000193623};
RN [1] {ECO:0000313|EMBL:SLN56379.1, ECO:0000313|Proteomes:UP000193623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8397 {ECO:0000313|EMBL:SLN56379.1,
RC ECO:0000313|Proteomes:UP000193623};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036490, 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; FWFT01000005; SLN56379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5T8T3; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000193623; 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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR011408; Aldehyde_DH.
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; 2.
DR PIRSF; PIRSF036490; Aldedh_dupl; 1.
DR SUPFAM; SSF53720; ALDH-like; 2.
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:UP000193623}.
FT DOMAIN 47..477
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 528..747
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 472..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 772 AA; 82268 MW; D01BD5D35B01B70B CRC64;
MTVKDIFDTM DYGPAPEDAS DARAWIEARG GIAGHFIGGT WDAMRADFDT TNPATGERLA
GVTKGTEAEV EKAVTAARKA QTKWAKNGKT RARVLYAIAR LMQKNARLLA VMETLDTGKP
IREARDIDVP LAIRHFYHHA GFAQLMDDEM PDVEPLGVCG QIIPWNFPLL MLAWKIAPAL
AMGNTVVLKP AEYTPMTAMI FAEICTQAGV PPGVVNIVTG DGETGAALVN ANVDKIAFTG
STAVGRLIRE QTAGTGKALS LELGGKSPYI VFEDADIDSA VEGLVDAIWF NGGQVCCAGS
RLLVQEGIAE TFYAKLKAHM DALRMGDPLD KCIDVGAIVD PSQLDRISSM VAQNTAGDTY
QCGAPDGCFY PPTLITGLAP SDTLMQEEIF GPVLVATTFR TPAEAVEVAN NTRYGLAASV
WSENINLALD IAPKLVSGIV WINGTNMMDA AAGFGGVRES GFGREGGWEG LQGYTKPRGK
PTPLKTPVTF TSDDGTPADP LDRTAKLYIG GKQARPDGGY SQPVFNKSGQ LLGHASIANR
KDLRNAAEAM AAAKGWSKTS GHLRAQILYY IGENLSARAD EFATRINALT GGRNGKAEVE
TAIDHLFTWA AWADKHDGAA KGVPIRGVAL AMNEPIGSIG VLTDDTRPLM GLIEPLAPAL
AMGNRLTAVA SHPFPLAATD FYQILETSDV PPGVVNILTG AHGDLAPHMA AHANIDAVWS
FSTSDVSKVI EARSAVTLKR TWVNNGTHRS WPSATWRAQA TEVKTIWIPY GE
//