GLPD_ECOLI
ID GLPD_ECOLI Reviewed; 501 AA.
AC P13035; P78115; Q2M790; Q47234;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE EC=1.1.5.3;
GN Name=glpD; Synonyms=glyD; OrderedLocusNames=b3426, JW3389;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1987111; DOI=10.1128/jb.173.1.101-107.1991;
RA Austin D., Larson T.J.;
RT "Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-
RT phosphate dehydrogenase of Escherichia coli K-12.";
RL J. Bacteriol. 173:101-107(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Choi Y.-L., Kawase S., Kawamukai M., Utsumi R., Sakai H., Komano T.;
RT "Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of
RT Escherichia coli and regulation by the cAMP-CRP complex.";
RL Agric. Biol. Chem. 53:1135-1143(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RC STRAIN=K12;
RX PubMed=3045087; DOI=10.1128/jb.170.9.4209-4215.1988;
RA Ye S., Larson T.J.;
RT "Structures of the promoter and operator of the glpD gene encoding aerobic
RT sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12.";
RL J. Bacteriol. 170:4209-4215(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RX PubMed=3045764; DOI=10.1093/nar/16.15.7732;
RA Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M.,
RA Utsumi R., Kohara Y., Akiyama K.;
RT "Nucleotide sequence of the glpR gene encoding the repressor for the
RT glycerol-3-phosphate regulon of Escherichia coli K12.";
RL Nucleic Acids Res. 16:7732-7732(1988).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC molecular oxygen or nitrate as electron acceptor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC route): step 1/1.
CC -!- INTERACTION:
CC P13035; P0AEE8: dam; NbExp=3; IntAct=EBI-548509, EBI-548491;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: There are two sn-glycerol-3-phosphate dehydrogenase
CC isozymes in E.coli: one is aerobic, the other anaerobic.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23888.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M55989; AAA24636.1; -; Genomic_DNA.
DR EMBL; M96795; AAC28164.1; -; Genomic_DNA.
DR EMBL; D00425; BAA00327.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58224.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76451.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77866.1; -; Genomic_DNA.
DR EMBL; M21277; AAA23885.1; -; Genomic_DNA.
DR EMBL; M54940; AAA23888.1; ALT_INIT; Genomic_DNA.
DR PIR; A39186; DEECGD.
DR RefSeq; NP_417884.1; NC_000913.3.
DR RefSeq; WP_000448136.1; NZ_SSZK01000008.1.
DR PDB; 2QCU; X-ray; 1.75 A; A/B=1-501.
DR PDB; 2R45; X-ray; 2.30 A; A/B=1-501.
DR PDB; 2R46; X-ray; 2.10 A; A/B=1-501.
DR PDB; 2R4E; X-ray; 2.10 A; A/B=1-501.
DR PDB; 2R4J; X-ray; 1.96 A; A/B=1-501.
DR PDBsum; 2QCU; -.
DR PDBsum; 2R45; -.
DR PDBsum; 2R46; -.
DR PDBsum; 2R4E; -.
DR PDBsum; 2R4J; -.
DR AlphaFoldDB; P13035; -.
DR SMR; P13035; -.
DR BioGRID; 4261265; 432.
DR DIP; DIP-9793N; -.
DR IntAct; P13035; 91.
DR STRING; 511145.b3426; -.
DR SWISS-2DPAGE; P13035; -.
DR jPOST; P13035; -.
DR PaxDb; P13035; -.
DR PRIDE; P13035; -.
DR EnsemblBacteria; AAC76451; AAC76451; b3426.
DR EnsemblBacteria; BAE77866; BAE77866; BAE77866.
DR GeneID; 947934; -.
DR KEGG; ecj:JW3389; -.
DR KEGG; eco:b3426; -.
DR PATRIC; fig|511145.12.peg.3521; -.
DR EchoBASE; EB0389; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_0_6; -.
DR InParanoid; P13035; -.
DR OMA; FAYSDCW; -.
DR PhylomeDB; P13035; -.
DR BioCyc; EcoCyc:AERGLYC3PDEHYDROG-MON; -.
DR BioCyc; MetaCyc:AERGLYC3PDEHYDROG-MON; -.
DR BRENDA; 1.1.5.3; 2026.
DR UniPathway; UPA00618; UER00674.
DR EvolutionaryTrace; P13035; -.
DR PRO; PR:P13035; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0052590; F:sn-glycerol-3-phosphate:ubiquinone oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IMP:EcoCyc.
DR Gene3D; 1.10.8.870; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; PTHR11985; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Glycerol metabolism;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..501
FT /note="Aerobic glycerol-3-phosphate dehydrogenase"
FT /id="PRO_0000126098"
FT BINDING 5..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 23
FT /note="A -> G (in Ref. 2; BAA00327)"
FT /evidence="ECO:0000305"
FT CONFLICT 328..353
FT /note="QAITRDYTLDIHDENGKAPLLSVFGG -> HVLPVITPLIFMMKMAKHRCCR
FT YSAA (in Ref. 2; BAA00327)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..501
FT /note="DDALWRRTKQGMWLNADQQSRVSQWLVEYTQQRLSLAS -> ARRPVASHKT
FT RHVAKCGSTISCESVAGGVYAAEVIAGVVN (in Ref. 2; BAA00327)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:2QCU"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:2QCU"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:2QCU"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:2QCU"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2QCU"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 463..468
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:2QCU"
FT HELIX 479..494
FT /evidence="ECO:0007829|PDB:2QCU"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:2QCU"
SQ SEQUENCE 501 AA; 56751 MW; 1C4D341E9E4536AB CRC64;
METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE
FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS
TGLRFGANSV LKPEIKRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATSARRENG
LWIVEAEDID TGKKYSWQAR GLVNATGPWV KQFFDDGMHL PSPYGIRLIK GSHIVVPRVH
TQKQAYILQN EDKRIVFVIP WMDEFSIIGT TDVEYKGDPK AVKIEESEIN YLLNVYNTHF
KKQLSRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK
LAEHALEKLT PYYQGIGPAW TKESVLPGGA IEGDRDDYAA RLRRRYPFLT ESLARHYART
YGSNSELLLG NAGTVSDLGE DFGHEFYEAE LKYLVDHEWV RRADDALWRR TKQGMWLNAD
QQSRVSQWLV EYTQQRLSLA S
