ID K9W512_9CYAN Unreviewed; 399 AA.
AC K9W512;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Glycerol dehydrogenase {ECO:0000313|EMBL:AFZ15286.1};
DE EC=1.1.1.6 {ECO:0000313|EMBL:AFZ15286.1};
GN ORFNames=Cri9333_4505 {ECO:0000313|EMBL:AFZ15286.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ15286.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ15286.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ15286.1,
RC ECO:0000313|Proteomes:UP000010472};
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 chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-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; CP003620; AFZ15286.1; -; Genomic_DNA.
DR RefSeq; WP_015205377.1; NC_019753.1.
DR AlphaFoldDB; K9W512; -.
DR STRING; 1173022.Cri9333_4505; -.
DR KEGG; cep:Cri9333_4505; -.
DR PATRIC; fig|1173022.3.peg.4867; -.
DR eggNOG; COG0371; Bacteria.
DR HOGENOM; CLU_044754_0_0_3; -.
DR OrthoDB; 5198708at2; -.
DR Proteomes; UP000010472; 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:AFZ15286.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 24..362
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT BINDING 108..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 139
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 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 185
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 263
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 280
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 399 AA; 42177 MW; C6E13D3084EE68E5 CRC64;
MPYQSSSALS SQTTNSLLCL TVAPSQVLQG TDALQQAKSA IARLGKRPLV VRGDRTLADT
PQLQPLLNME LQVAEAAYIP DCSEASLESL KQAVANHQAD VIIGVGGGKA LDTAKLIAYQ
CQLPVVTIPT SAATCAAWTA LSNVYSDEGA FLYDVSLLKC PDLLILDYNL IQTAPQRTLV
AGIGDAIAKW YEASVSSGNS EQTLIIAAVQ QARVLRDLLF QKSAAALKEP GSTVWQEVVN
ATVLLAGVIG GLGGAQCRTV AAHAVHNGLT HLPGSHNALH GEKVAYGILV QLRLEEMVQG
NKLAATARQQ LLKFYAEINL PQTLDDLGLG EITLTQLRHA AEIACNPNSD IHRLPFQIVP
DQLMAAMVST TTPVETGRSN LGIAAINSTA NQGCEDTDS
//
