ID   D5BRV0_PUNMI            Unreviewed;       480 AA.
AC   D5BRV0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Aldehyde dehydrogenase family protein {ECO:0000313|EMBL:ADE38997.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:ADE38997.1};
GN   OrderedLocusNames=SAR116_0754 {ECO:0000313|EMBL:ADE38997.1};
OS   Puniceispirillum marinum (strain IMCC1322).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC   Puniceispirillum.
OX   NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE38997.1, ECO:0000313|Proteomes:UP000007460};
RN   [1] {ECO:0000313|EMBL:ADE38997.1, ECO:0000313|Proteomes:UP000007460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE38997.1,
RC   ECO:0000313|Proteomes:UP000007460};
RX   PubMed=20382761; DOI=10.1128/JB.00347-10;
RA   Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT   "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT   IMCC1322, a representative of the SAR116 clade in the
RT   Alphaproteobacteria.";
RL   J. Bacteriol. 192:3240-3241(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00024149};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP001751; ADE38997.1; -; Genomic_DNA.
DR   RefSeq; WP_013045626.1; NC_014010.1.
DR   AlphaFoldDB; D5BRV0; -.
DR   STRING; 488538.SAR116_0754; -.
DR   KEGG; apb:SAR116_0754; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_5; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000007460; Chromosome.
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   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   CDD; cd07138; ALDH_CddD_SSP0762; 1.
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; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 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:UP000007460}.
FT   DOMAIN          13..474
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   480 AA;  51180 MW;  0A6EEDAC55AE9E48 CRC64;
     MIDKTDLYID GEWVKSIDGR VVPVINPATE EEYASITLAG KADTESAIAA AKRAFPAWSM
     TSPEERLDYL KKLLEVYQAR EREMAHTISD EMGAPIDLAI SEQASSGSSH LKAFIRTLAA
     FEWVRPLRPG TAGQDLTYEP AGVAALITPW NWPMNQVVLK VGAAIAAGCT MVLKPSEIAP
     MSGMLFAEMV HEVGLPAGVF NLINGDGVGA GSIMSSHPDI DVVSFTGSTR AGILITKAAA
     DSVKNVSLEL GGKSPNLIFD DCDIEAAVTR GTKFCFNNTG QSCNAATRML VERSAYDQAV
     EVAARVADET KVDMPSKEGK HIGPLVSEAQ FNKVQDLIQK GIDEGARLVA GGVGRPDGLN
     RGYFVRPTVF ADTNNDMTIM REEIFGPVLS IMPFDTEDEA IAIANDTPFG LSAYLQTGDT
     ERAHRVARQL RAGMVQVNGA SRASGSPFGG FKQSGVGREG GAMGIEEFLE VKTISGIVDA
//