[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=1987111 [NCBI, ExPASy, EBI, Israel, Japan] Austin D., Larson T.J.; "Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12."; J. Bacteriol. 173:101-107(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Choi Y.-L., Kawase S., Kawamukai M., Utsumi R., Sakai H., Komano T.; "Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of Escherichia coli and regulation by the cAMP-CRP complex."; Agric. Biol. Chem. 53:1135-1143(1989).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61. STRAIN=K12; PubMed=3045087 [NCBI, ExPASy, EBI, Israel, Japan] Ye S., Larson T.J.; "Structures of the promoter and operator of the glpD gene encoding aerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12."; J. Bacteriol. 170:4209-4215(1988).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61. DOI=10.1093/nar/16.15.7732; PubMed=3045764 [NCBI, ExPASy, EBI, Israel, Japan] Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M., Utsumi R., Kohara Y., Akiyama K.; "Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12."; Nucleic Acids Res. 16:7732-7732(1988).

Comments

FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor.
CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor.
COFACTOR: FAD.
PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic route): step 1/1 .
INTERACTION:
P0ACS9:acrR; NbExp=1; IntAct=EBI-548509, EBI-1117360;
P69330:citD; NbExp=1; IntAct=EBI-548509, EBI-1119230;
P0A9K7:phoU; NbExp=1; IntAct=EBI-548509, EBI-1133614;
P0A8D3:yaiI; NbExp=1; IntAct=EBI-548509, EBI-1116378;
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: There are two sn-glycerol-3-phosphate dehydrogenase isozymes in E.coli: one is aerobic, the other anaerobic.
SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M55989; AAA24636.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M96795; AAC28164.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00425; BAA00327.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58224.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76451.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77866.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21277; AAA23885.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M54940; AAA23888.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39186; DEECGD.

RefSeq

AP_004365.1; -.
NP_417884.1; -.

3D structure databases

PDB

2QCU; X-ray; 1.75 A; A/B=1-501.	[ExPASy / RCSB / EBI]
2R45; X-ray; 2.30 A; A/B=1-501.	[ExPASy / RCSB / EBI]
2R46; X-ray; 2.10 A; A/B=1-501.	[ExPASy / RCSB / EBI]
2R4E; X-ray; 2.10 A; A/B=1-501.	[ExPASy / RCSB / EBI]
2R4J; X-ray; 1.96 A; A/B=1-501.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2QCU; -.
2R45; -.
2R46; -.
2R4E; -.
2R4J; -.

ModBase

P13035.

Protein-protein interaction databases

DIP

DIP:9793N; -.

IntAct

P13035; -.

Enzyme and pathway databases

BioCyc

EcoCyc:AERGLYC3PDEHYDROG-MON; -.
MetaCyc:AERGLYC3PDEHYDROG-MON; -.

2D gel databases

SWISS-2DPAGE

P13035; -.

ECO2DBASE

H047.3; 6TH EDITION.

Organism-specific databases

EchoBASE

EB0389; -.

EcoGene

EG10394; glpD.

Ontologies

GO:0009331;	Cellular component: glycerol-3-phosphate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004368;	Molecular function: glycerol-3-phosphate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006072;	Biological process: glycerol-3-phosphate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000447; FAD-dep_Gly3P_DHase.
IPR006076; FAD-dep_OxRdtase.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

PRINTS

PR01001; FADG3PDH.

PROSITE

PS00977; FAD_G3PDH_1; 1.
PS00978; FAD_G3PDH_2; 1.

ProtoNet

P13035.

Genome annotation databases

GeneID

947934; -.

GenomeReviews

U00096_GR; b3426.
AP009048_GR; JW3389.

KEGG

ecj:JW3389; -.
eco:b3426; -.

Phylogenomic databases

HOGENOM

P13035; -.

Genome annotation databases

CMR

P13035; b3426.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 501`	`501`	`Aerobic glycerol-3-phosphate dehydrogenase.`	`PRO_0000126098`
`NP_BIND`	`5 33`	`29`	`FAD (Potential).`
`CONFLICT`	`23 23`		`A -> G (in Ref. 2; BAA00327).`
`CONFLICT`	`328 353`		`QAITRDYTLDIHDENGKAPLLSVFGG -> HVLPVITPLIFMMKMAKHRCCRYSAA (in Ref. 2; BAA00327).`
`CONFLICT`	`464 501`		`DDALWRRTKQGMWLNADQQSRVSQWLVEYTQQRLSLAS -> ARRPVASHKTRHVAKCGSTISCESVAGGVYAAEVIAGVVN (in Ref. 2; BAA00327).`
`STRAND`	`4 9`	`6`
`HELIX`	`13 24`	`12`
`STRAND`	`29 32`	`4`
`STRAND`	`34 36`	`3`
`HELIX`	`41 43`	`3`
`HELIX`	`53 58`	`6`
`HELIX`	`61 77`	`17`
`TURN`	`79 81`	`3`
`STRAND`	`82 90`	`9`
`TURN`	`93 95`	`3`
`HELIX`	`98 109`	`12`
`STRAND`	`110 112`	`3`
`STRAND`	`115 117`	`3`
`STRAND`	`121 124`	`4`
`STRAND`	`129 131`	`3`
`STRAND`	`137 146`	`10`
`HELIX`	`148 161`	`14`
`STRAND`	`165 167`	`3`
`STRAND`	`169 178`	`10`
`STRAND`	`181 188`	`8`
`TURN`	`189 191`	`3`
`STRAND`	`194 200`	`7`
`STRAND`	`202 204`	`3`
`HELIX`	`207 209`	`3`
`HELIX`	`210 216`	`7`
`STRAND`	`229 237`	`9`
`STRAND`	`239 241`	`3`
`STRAND`	`245 249`	`5`
`STRAND`	`255 261`	`7`
`TURN`	`262 264`	`3`
`STRAND`	`265 269`	`5`
`HELIX`	`279 281`	`3`
`HELIX`	`286 299`	`14`
`STRAND`	`300 302`	`3`
`HELIX`	`306 308`	`3`
`STRAND`	`311 317`	`7`
`HELIX`	`327 329`	`3`
`STRAND`	`335 341`	`7`
`STRAND`	`344 351`	`8`
`HELIX`	`355 357`	`3`
`HELIX`	`358 369`	`12`
`HELIX`	`370 372`	`3`
`HELIX`	`381 383`	`3`
`STRAND`	`391 393`	`3`
`TURN`	`394 397`	`4`
`HELIX`	`398 405`	`8`
`HELIX`	`411 420`	`10`
`HELIX`	`422 424`	`3`
`HELIX`	`425 429`	`5`
`HELIX`	`435 438`	`4`
`HELIX`	`448 457`	`10`
`HELIX`	`463 468`	`6`
`HELIX`	`473 475`	`3`
`HELIX`	`479 494`	`16`
`STRAND`	`495 498`	`4`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 56751 Da [This is the MW of the unprocessed precursor]

CRC64: 1C4D341E9E4536AB [This is a checksum on the sequence]

        10         20         30         40         50         60 
METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE 

        70         80         90        100        110        120 
FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS 

       130        140        150        160        170        180 
TGLRFGANSV LKPEIKRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATSARRENG 

       190        200        210        220        230        240 
LWIVEAEDID TGKKYSWQAR GLVNATGPWV KQFFDDGMHL PSPYGIRLIK GSHIVVPRVH 

       250        260        270        280        290        300 
TQKQAYILQN EDKRIVFVIP WMDEFSIIGT TDVEYKGDPK AVKIEESEIN YLLNVYNTHF 

       310        320        330        340        350        360 
KKQLSRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK 

       370        380        390        400        410        420 
LAEHALEKLT PYYQGIGPAW TKESVLPGGA IEGDRDDYAA RLRRRYPFLT ESLARHYART 

       430        440        450        460        470        480 
YGSNSELLLG NAGTVSDLGE DFGHEFYEAE LKYLVDHEWV RRADDALWRR TKQGMWLNAD 

       490        500 
QQSRVSQWLV EYTQQRLSLA S

P13035 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools