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Database: UniProt
Entry: A0A132C1T2_9RHOB
LinkDB: A0A132C1T2_9RHOB
Original site: A0A132C1T2_9RHOB 
ID   A0A132C1T2_9RHOB        Unreviewed;       504 AA.
AC   A0A132C1T2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Lactaldehyde dehydrogenase {ECO:0000313|EMBL:KUP94561.1};
DE            EC=1.2.1.21 {ECO:0000313|EMBL:KUP94561.1};
DE            EC=1.2.1.22 {ECO:0000313|EMBL:KUP94561.1};
GN   Name=aldA_1 {ECO:0000313|EMBL:KUP94561.1};
GN   ORFNames=TRIHO_04870 {ECO:0000313|EMBL:KUP94561.1};
OS   Tritonibacter horizontis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tritonibacter.
OX   NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP94561.1, ECO:0000313|Proteomes:UP000068382};
RN   [1] {ECO:0000313|EMBL:KUP94561.1, ECO:0000313|Proteomes:UP000068382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O3.65 {ECO:0000313|EMBL:KUP94561.1,
RC   ECO:0000313|Proteomes:UP000068382};
RA   Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT   "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT   Tritonibacter horizontis.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, 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:KUP94561.1}.
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DR   EMBL; LPUY01000012; KUP94561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A132C1T2; -.
DR   PATRIC; fig|1768241.3.peg.494; -.
DR   Proteomes; UP000068382; Unassembled WGS sequence.
DR   GO; GO:0050569; F:glycolaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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:UP000068382}.
FT   DOMAIN          19..480
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   504 AA;  53869 MW;  B1B74C9BF2D4C6DB CRC64;
     MDFSATGGIA AHMLIDGQWI APRAGAVIAV DNPADETVIG TIPEGTAQDA ARAIDAAHRA
     QPAWAALPAV DRGRAVRKLA ALVAERTEEL ARLITREQGK PIGQARGEVG AVVGFLEHAA
     ENARRIEGDI VASDNRDEEI HIRRHPYGVV VGLTAWNYPA ALAARKIGPA LVAGNSFVLL
     GHEITPFSGL FIAALAEKAG IPRGVINVVT GRGAVVGQAL VEHPETALVT MTGSNRAGQQ
     IFRSAAEGMK VLRLELGGKA PFIVMEDAEI DRAVAAAVTA RYTNCGQICT CNERMYLHQD
     IADEFLEKFV AASKALRIGD PMGDPDMGPK VSAGEVAKVQ SIVDAAVAQG AEVLLQGGPL
     NDGPYAKGHW IAPTILEVRD NASPVMGQEV FGPVAPVMRV PDFDTALAMA NDTAFGLSAY
     VFTQDHRRLM QTPYRLKFGE IYVNRANGEQ FQAFHNGWGH SGLGGEDGKY GFDGYLRKQT
     LYMNWGYPVR RGQGGLAAHW EEKT
//
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