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Database: UniProt
Entry: Q2JPP3_SYNJB
LinkDB: Q2JPP3_SYNJB
Original site: Q2JPP3_SYNJB 
ID   Q2JPP3_SYNJB            Unreviewed;       876 AA.
AC   Q2JPP3;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   OrderedLocusNames=CYB_0241 {ECO:0000313|EMBL:ABD01239.1};
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD01239.1, ECO:0000313|Proteomes:UP000001938};
RN   [1] {ECO:0000313|EMBL:ABD01239.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JA-2-3B'a;
RA   Heidelberg J.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABD01239.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JA-2-3B'a;
RX   PubMed=16391090; DOI=10.1128/AEM.72.1.544-550.2006;
RA   Allewalt J.P., Bateson M.M., Revsbech N.P., Slack K., Ward D.M.;
RT   "Effect of temperature and light on growth of and photosynthesis by
RT   Synechococcus isolates typical of those predominating in the octopus spring
RT   microbial mat community of Yellowstone National Park.";
RL   Appl. Environ. Microbiol. 72:544-550(2006).
RN   [3] {ECO:0000313|EMBL:ABD01239.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a {ECO:0000313|EMBL:ABD01239.1};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC       alcohol dehydrogenase family. {ECO:0000256|ARBA:ARBA00035645,
CC       ECO:0000256|PIRNR:PIRNR000111}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00035641,
CC       ECO:0000256|PIRNR:PIRNR000111}.
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DR   EMBL; CP000240; ABD01239.1; -; Genomic_DNA.
DR   RefSeq; WP_011431908.1; NC_007776.1.
DR   AlphaFoldDB; Q2JPP3; -.
DR   STRING; 321332.CYB_0241; -.
DR   KEGG; cyb:CYB_0241; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_1_1_3; -.
DR   OMA; QWFKVPP; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   CDD; cd08178; AAD_C; 1.
DR   CDD; cd07122; ALDH_F20_ACDH; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR034789; AAD_C.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012079; Bifunc_Ald-ADH.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PIRSF; PIRSF000111; ALDH_ADH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001938}.
FT   DOMAIN          5..400
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          456..849
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   876 AA;  96074 MW;  D4CC49F4D33987B1 CRC64;
     MPVTNLAELE TLIQQVKAAQ AEYATFTQEQ VDRIFHKAAL AANNERIPLA KLAVQETGMG
     IVEDKVIKNH FASEYIYNKY KHEKTCGVIE RDESFGYERI AEPVGLLAGI VPVTNPTSTT
     IFKALITLKT RNGIIFSPHP RAKKCTIAAA KVVKEAAEAA GAPVGLIGWI DEPTIELSQA
     LMQHPEVKLI LATGGPGMVK AAYSSGHPSL GVGAGNTPAV IDASADIPMA VSSILLSKTF
     DNGMICASEQ AVVVVDAIYE QVKAEFGHRG AYILDPEQIE AVRRILLKDG RLNPAIVGQS
     VQTIAALAGI QVPEGTKLLI GEVEKVGPEE PFSYEKLAPV LALYRANDFH SAVDVAVQLV
     NFGGRGHTSV LYTDPANRDD IAYFENALQT GRVLINTPSS QGAIGDLYNF KLDPSLTLGC
     GTWGGNSISE NVGPRHLLNI KTVTQRRENM LWFRIPPKVY FKPGCLPIAL RELAGKKRAF
     LVTDKPLFEL GILHPITQVL DEIRVSWDVY HDVEPDPTLS NVNRGLEQLR QFQPDVIIAV
     GGGSPMDAAK VMWLMYEQPQ VEFEGLAMRF MDIRKRVYEL PPLGQKAQLI CIPTTSGTGS
     EVTPFAVVTD DRVGIKYPLA DYALTPTMAI VDPDLTLKMP KKLTAYGGID ALTHALEAYV
     SVMASDFTDG LALQAIKLLM TYLPRAYEKG AEDPEAREKV HYAATIAGMA FANAFLGVCH
     SLAHKLGSTF HLPHGLANAL MITHVIRYNA TDAPFKQAIF PQYRYPNAKH RYAEIADYLQ
     LGGADDDEKV MRLIEAIEEL KRKLGIPATI REALGEKERE FYDRLEAMAE QAFDDQCTGA
     NPRYPLIQDM KELYVLAYRG CRVDSALYHQ PEPVLA
//
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