ID A0A0N0D845_9RHOB Unreviewed; 781 AA.
AC A0A0N0D845;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Putative aldehyde dehydrogenase AldA {ECO:0000313|EMBL:KPA20511.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:KPA20511.1};
GN Name=aldA {ECO:0000313|EMBL:KPA20511.1};
GN ORFNames=shim_35010 {ECO:0000313|EMBL:KPA20511.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA20511.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA20511.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA20511.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036490, 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:KPA20511.1}.
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; LAJH01000021; KPA20511.1; -; Genomic_DNA.
DR RefSeq; WP_054003895.1; NZ_LAJH01000021.1.
DR AlphaFoldDB; A0A0N0D845; -.
DR STRING; 1389006.shim_35010; -.
DR PATRIC; fig|1389006.3.peg.3608; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000037951; 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 CDD; cd07111; ALDH_F16; 1.
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:UP000037951}.
FT DOMAIN 41..483
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 531..749
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 781 AA; 83502 MW; F43802D6AE0FE594 CRC64;
MTVKEIFETM NYGPAPESAG DALAWIVDQG AAFGQFIDGD WTEPRKDFQS KNPANGETLA
DLTQASQDEI NAAVAAARKA QSKWEGLGGH GRAKYLYAIA RLLQKHSRLF AVLETLDNGK
PIRESRDIDI PLVQRHFYYH AGMAQLMESE LPDAQALGVC GQIIPWNFPL LMLAWKVAPA
LAMGNTVVLK PAEYTSLTAL LFADICQQAG LPAGVVNIVT GDGAVGEMIT AHEDVNKVAF
TGSTDVGKRI RHSTAGSGKS LTLELGGKSP YIVFDDADID SAIEGLVDAI WFNQGQVCCA
GSRLLVQEGI ADTFHRKLKA RMDGLRIGNP LDKCIDVGAI VDPVQLKTIS DLVDGNSEGE
TYQPALDMPT EGCFYPPTLI TGLAPSSKLM QEEIFGPVLV STTFRTPSEV VALANNTRYG
LAATLWTENV NLALDIAPKL VAGVVWINAT NLFDAAAGFG GVRESGYGRE GGWEGLSAYT
KPKGSAKAIK PVEAFSGDKG PLDPLDRTPK LYIGGKQARP DSGYSQSIFG KNGALLGQVP
IANRKDVRNA VEAAHAAKGW SGTTGHLRAQ ILYFIAENLS ARREEFANRI NTLKGGKTGD
KEVDTSIRRL FTYAAWADKY DGQAHGVPIR GVALAMKEPV GVIGALCPDD LPLLGLISAM
APAIAMGNRV VLAASQTFPL AATDFYQVLE TSDLPGGVVN ILTGSHAELA KPLAGHMDVD
AVWSFSGADV SAEIERESAG NLKRTWVNNG MARDWMGAEG EGRTFLQAAT EVKNIWVPYG
E
//