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Database: UniProt
Entry: A0A0N0D845_9RHOB
LinkDB: A0A0N0D845_9RHOB
Original site: A0A0N0D845_9RHOB 
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}.
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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
//
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