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Database: UniProt
Entry: K2J837_9RHOB
LinkDB: K2J837_9RHOB
Original site: K2J837_9RHOB 
ID   K2J837_9RHOB            Unreviewed;       781 AA.
AC   K2J837;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:EKE71368.1};
GN   ORFNames=B30_11405 {ECO:0000313|EMBL:EKE71368.1};
OS   Celeribacter baekdonensis B30.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE71368.1, ECO:0000313|Proteomes:UP000006762};
RN   [1] {ECO:0000313|EMBL:EKE71368.1, ECO:0000313|Proteomes:UP000006762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B30 {ECO:0000313|EMBL:EKE71368.1,
RC   ECO:0000313|Proteomes:UP000006762};
RA   Wang W.;
RT   "Celeribacter baekdonensis B30 Genome Sequencing.";
RL   Submitted (SEP-2012) 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:EKE71368.1}.
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DR   EMBL; AMRK01000005; EKE71368.1; -; Genomic_DNA.
DR   RefSeq; WP_009572231.1; NZ_AMRK01000005.1.
DR   AlphaFoldDB; K2J837; -.
DR   STRING; 1208323.B30_11405; -.
DR   PATRIC; fig|1208323.3.peg.2363; -.
DR   eggNOG; COG1012; Bacteria.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000006762; 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:UniProtKB-UniRule.
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; 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; 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:UP000006762}.
FT   DOMAIN          52..486
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          536..755
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   781 AA;  83294 MW;  49854BB414A6ED65 CRC64;
     MTVKEIFETM DYGAAPESAA EALAWLVEGG DRFGHFIDGK MTAPATAPGE VFLAKNPATG
     EVLAHLTQAS LGEVDMAVAA ARKAQAKWEK RGGKARAKVL YALARLVQKH ARLFAVLETL
     DNGKPIRESR DIDVALVARH FYYHAGMAQL MDEELPNRAA LGVCGQIIPW NFPLLMLAWK
     VAPAIAMGNT VVLKPAEYTS LTALLFAQIC QEAGVPKGVV NIVTGDGAVG EMIVTHPDID
     KIAFTGSTAV GRRIRQATAG SGKSLTLELG GKSPYIVFED ADIDSAIEGL VDAIFFNQGQ
     VCCAGSRLLV QEGIAEDFHA RLIDRMSKLR IGNPLDKCID VGAIVDPKQL ERIEALIAKG
     GMEGTVNQPC PAPEGCFYPP TLISGLHPSA MLMQEEIFGP VLVSTTFRTP EEAVQVANNT
     RFGLAASVWS ENVNLALDIA PKLVAGVVWV NGSNMFDAAA GFGGVRESGF GREGGWEGLM
     AYTKPKGKVT TVKPAMAHSK PDTVEVLNLD RTAKLYIGGK QARPDSGYSQ AIYAPKGTLL
     GHASLASRKD IRNAVEAAQG AKGWSKTTAH NRAQVLYFVG ENLSARADEF AQRIRDLTGT
     TEAKAKEEVA EAIDTLFTFA AWADKLDGAA KPVPMRGVAL AMNEAVGVIG AFCDDRPLGG
     LIDVIAPAIA MGNRVVAVAS EAYPLAATDF YQVLDTSDVP AGVVNILTGS HSDLAKPMAG
     HMDLEAVWSF SGADISKTIE LESAGNLKRT WVNFGQTRTY AARDWLAQAT EVKTIWVPYG
     E
//
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