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Database: UniProt
Entry: F6CVG5_MARPP
LinkDB: F6CVG5_MARPP
Original site: F6CVG5_MARPP 
ID   F6CVG5_MARPP            Unreviewed;       482 AA.
AC   F6CVG5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Salicylaldehyde dehydrogenase {ECO:0000313|EMBL:AEF55342.1};
DE            EC=1.2.1.65 {ECO:0000313|EMBL:AEF55342.1};
GN   OrderedLocusNames=Mar181_2306 {ECO:0000313|EMBL:AEF55342.1};
OS   Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF55342.1, ECO:0000313|Proteomes:UP000009230};
RN   [1] {ECO:0000313|EMBL:AEF55342.1, ECO:0000313|Proteomes:UP000009230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC   {ECO:0000313|Proteomes:UP000009230};
RX   PubMed=23458837; DOI=10.4056/sigs.2976373;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA   Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT   "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT   181(T)).";
RL   Stand. Genomic Sci. 7:31-43(2012).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP002771; AEF55342.1; -; Genomic_DNA.
DR   RefSeq; WP_013796817.1; NC_015559.1.
DR   AlphaFoldDB; F6CVG5; -.
DR   STRING; 491952.Mar181_2306; -.
DR   KEGG; mpc:Mar181_2306; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000009230; Chromosome.
DR   GO; GO:0018485; F:salicylaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd07105; ALDH_SaliADH; 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; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR42986; BENZALDEHYDE DEHYDROGENASE YFMT; 1.
DR   PANTHER; PTHR42986:SF1; BENZALDEHYDE DEHYDROGENASE YFMT; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          16..471
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   482 AA;  50655 MW;  67873BB347601E6F CRC64;
     MTTVLLSIGG KDRAASHAKT YSRLDPVTRD VASVCAAASL EDVASVTKAA DEAFVNWSTV
     GPSERRVLLN EAANIMEAKV DDFISAMIAE TGATGPWAGF NVMLAAGHIR EAAALTTQVG
     GEVIPANKPG TLAMSINKPK GVCLAIAPWN APVILGARAI ATPLACGNTV ILKSSEFCPL
     THRLIIDCFL EAGFPAGVIN LLSNDPSDAP DIVKALIEAP EVRHVNFTGS SPVGRIIGRL
     AGENLKPALL ELGGKAPLVV LADADIEAAV NAAIFGAFMN QGQICMSTER MIVDDSIADE
     FVDQLIARAS TLPWGNPREQ VVLGSLVNPE AADKMRQLID DAVSKGAKLV CGGENDGAIF
     SATLLDCVND QMRIYREESF GPVKSIIRVN GDAEAIKVAN DSEYGLSAAL FSQNINRALA
     CANAIKSGIC HINGPTLADE PQMPFGGVGD SGYGRFGGKA GIAEFTDVRW ITIEDAKQHY
     PF
//
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