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
//