GLDA_THEMA
ID GLDA_THEMA Reviewed; 364 AA.
AC Q9WYQ4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glycerol dehydrogenase;
DE Short=GDH;
DE Short=GLDH;
DE EC=1.1.1.6;
GN Name=gldA; OrderedLocusNames=TM_0423;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE
RP ANALOG.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=12193646; DOI=10.1073/pnas.142413399;
RA Lesley S.A., Kuhn P., Godzik A., Deacon A.M., Mathews I., Kreusch A.,
RA Spraggon G., Klock H.E., McMullan D., Shin T., Vincent J., Robb A.,
RA Brinen L.S., Miller M.D., McPhillips T.M., Miller M.A., Scheibe D.,
RA Canaves J.M., Guda C., Jaroszewski L., Selby T.L., Elsliger M.-A.,
RA Wooley J., Taylor S.S., Hodgson K.O., Wilson I.A., Schultz P.G.,
RA Stevens R.C.;
RT "Structural genomics of the Thermotoga maritima proteome implemented in a
RT high-throughput structure determination pipeline.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11664-11669(2002).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of glycerol to
CC dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol
CC as a source of carbon under anaerobic conditions (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 1/2.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35508.1; -; Genomic_DNA.
DR PIR; G72378; G72378.
DR RefSeq; NP_228233.1; NC_000853.1.
DR RefSeq; WP_004083283.1; NZ_CP011107.1.
DR PDB; 1KQ3; X-ray; 1.50 A; A=1-364.
DR PDBsum; 1KQ3; -.
DR AlphaFoldDB; Q9WYQ4; -.
DR SMR; Q9WYQ4; -.
DR STRING; 243274.THEMA_02610; -.
DR EnsemblBacteria; AAD35508; AAD35508; TM_0423.
DR KEGG; tma:TM0423; -.
DR eggNOG; COG0371; Bacteria.
DR InParanoid; Q9WYQ4; -.
DR OMA; ALHGEQC; -.
DR OrthoDB; 717704at2; -.
DR BRENDA; 1.1.1.6; 6331.
DR UniPathway; UPA00617; UER00668.
DR EvolutionaryTrace; Q9WYQ4; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; PTHR43616; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycerol metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..364
FT /note="Glycerol dehydrogenase"
FT /id="PRO_0000350665"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 92..96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 114..117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12193646"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12193646"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12193646"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 160..183
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 195..220
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 226..246
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:1KQ3"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1KQ3"
FT HELIX 343..360
FT /evidence="ECO:0007829|PDB:1KQ3"
SQ SEQUENCE 364 AA; 39692 MW; B44E20CACC6F1582 CRC64;
MITTTIFPGR YVQGAGAINI LEEELSRFGE RAFVVIDDFV DKNVLGENFF SSFTKVRVNK
QIFGGECSDE EIERLSGLVE EETDVVVGIG GGKTLDTAKA VAYKLKKPVV IVPTIASTDA
PCSALSVIYT PNGEFKRYLF LPRNPDVVLV DTEIVAKAPA RFLVAGMGDA LATWFEAESC
KQKYAPNMTG RLGSMTAYAL ARLCYETLLE YGVLAKRSVE EKSVTPALEK IVEANTLLSG
LGFESGGLAA AHAIHNGLTV LENTHKYLHG EKVAIGVLAS LFLTDKPRKM IEEVYSFCEE
VGLPTTLAEI GLDGVSDEDL MKVAEKACDK NETIHNEPQP VTSKDVFFAL KAADRYGRMR
KNLT
