ID K9QG79_9NOSO Unreviewed; 395 AA.
AC K9QG79;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Glycerol dehydrogenase {ECO:0000313|EMBL:AFY44343.1};
DE EC=1.1.1.6 {ECO:0000313|EMBL:AFY44343.1};
GN ORFNames=Nos7107_3782 {ECO:0000313|EMBL:AFY44343.1};
OS Nostoc sp. PCC 7107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY44343.1, ECO:0000313|Proteomes:UP000010381};
RN [1] {ECO:0000313|EMBL:AFY44343.1, ECO:0000313|Proteomes:UP000010381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY44343.1,
RC ECO:0000313|Proteomes:UP000010381};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Nostoc sp. PCC 7107.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-1};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; CP003548; AFY44343.1; -; Genomic_DNA.
DR RefSeq; WP_015114545.1; NC_019676.1.
DR AlphaFoldDB; K9QG79; -.
DR STRING; 317936.Nos7107_3782; -.
DR KEGG; nos:Nos7107_3782; -.
DR PATRIC; fig|317936.3.peg.4100; -.
DR eggNOG; COG0371; Bacteria.
DR HOGENOM; CLU_044754_0_0_3; -.
DR InParanoid; K9QG79; -.
DR OrthoDB; 5198708at2; -.
DR Proteomes; UP000010381; Chromosome.
DR GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08550; GlyDH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR PANTHER; PTHR43616:SF3; HYDROXYCARBOXYLATE DEHYDROGENASE A; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000112-1}; NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AFY44343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010381};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 24..363
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 110..114
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 187
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 265
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 281
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 395 AA; 41584 MW; 3F11DC41442E85E8 CRC64;
MPHQSTTTLS TQTSNSLPAL AIAPAKVIRG SGVLPAALAE IALLGSRPLI VAGNQTIALT
QDALQPILEQ QQLHTAQASY GADCSEASLK SLKKAAKEHK ADLIIGVGGG KALDTAKLVA
HQLQLPVVTI PTSAATCAAW TALSNVYSET GAFLYDVALS RCPDLLILDY DLIQTAPQHT
LVAGIGDAIA KWYEASVSSG HLQQTLIIAA VQQARVLRDI LFQKSAAALQ KPGSEVWQEV
VDATVLLAGV IGGLGGAQCR TVAAHAVHNG LTHIAGHSSI HGEKVAFGIL VQLRLEEMIL
GNQLATTARQ QLLKFYAEIG LPQKLDDLGL GNVKLSELKT AAEISLAPNS DIHRLPFKVG
IEQLMAAMVS TTAPTDSREC SNRVAARAIE EQIQE
//
