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Database: UniProt
Entry: M0CI10_9EURY
LinkDB: M0CI10_9EURY
Original site: M0CI10_9EURY 
ID   M0CI10_9EURY            Unreviewed;       360 AA.
AC   M0CI10;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=glycerol dehydrogenase {ECO:0000256|ARBA:ARBA00039147};
DE            EC=1.1.1.6 {ECO:0000256|ARBA:ARBA00039147};
GN   ORFNames=C475_17238 {ECO:0000313|EMBL:ELZ22278.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ22278.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ22278.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ22278.1,
RC   ECO:0000313|Proteomes:UP000011626};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH;
CC         Xref=Rhea:RHEA:13769, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036918};
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   -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC       from glycerol (oxidative route): step 1/2.
CC       {ECO:0000256|ARBA:ARBA00037918}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007358}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELZ22278.1}.
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DR   EMBL; AOIU01000036; ELZ22278.1; -; Genomic_DNA.
DR   RefSeq; WP_006885114.1; NZ_AOIU01000036.1.
DR   AlphaFoldDB; M0CI10; -.
DR   STRING; 797114.C475_17238; -.
DR   PATRIC; fig|797114.5.peg.3509; -.
DR   eggNOG; arCOG00982; Archaea.
DR   OrthoDB; 116813at2157; -.
DR   Proteomes; UP000011626; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08170; GlyDH; 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:SF5; GLYCEROL DEHYDROGENASE 1; 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   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000112-1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000112-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011626};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   DOMAIN          8..340
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   BINDING         96..100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         118..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         123
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         173
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         256
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         271
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   360 AA;  36508 MW;  E8CD473D63960C6E CRC64;
     MHRRFVSPRA YVQGAGALGD AGTEFDRLDA DRAVVLGGDT ALATVGDAVS TGLADAGIEV
     AHTAAGVDRC TDPALDDHVD AATTAGADLV VGVGGGVAMD VATAVADRIG ATLAVVPTIA
     STDAPTSTVA VVYDDAGNFR EVRYRDRNPE LVLVDTAVVA AAPARFLAYG MGDAIATRFE
     AEAVAATGGR TDADGESSFA AQALAEEAYG RVREHGPDAL AAVRRDAVTP AVERVVEANT
     LLSGLGFESG GTAGAHAVQI GLTDAGVREP HGLLVGFGTV AELVCRGAGP GTISEVLDLL
     FDIGLDVTLA ELGVGEDGLI TVGEVACEHG MDLEPVDATP RRVADAVRTA DELIRERRGG
//
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