Reviewed, UniProtKB/Swiss-Prot P13035 (GLPD_ECOLI)

Names and origin

Protein names

Recommended name:
    Aerobic glycerol-3-phosphate dehydrogenase
    EC=1.1.5.3

Gene names

Name:	glpD
Synonyms:	glyD
Ordered Locus Names:	b3426, JW3389

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor.
Catalytic activity	sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
Cofactor	FAD.
Pathway	Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic route): step 1/1.
Subcellular location	Cytoplasm.
Miscellaneous	There are two sn-glycerol-3-phosphate dehydrogenase isozymes in E.coli: one is aerobic, the other anaerobic.
Sequence similarities	Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycerol metabolism
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycerol-3-phosphate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	glycerol-3-phosphate dehydrogenase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
acrR	P0ACS9	1	EBI-548509,EBI-1117360
citD	P69330	1	EBI-548509,EBI-1119230
phoU	P0A9K7	1	EBI-548509,EBI-1133614
yaiI	P0A8D3	1	EBI-548509,EBI-1116378

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 501

501

Aerobic glycerol-3-phosphate dehydrogenase

PRO_0000126098

Regions

Nucleotide binding

5 – 33

29

FAD Potential

Experimental info

Sequence conflict

23

1

A → G in BAA00327. Ref.2

Sequence conflict

328 – 353

26

QAITR…SVFGG → HVLPVITPLIFMMKMAKHRC CRYSAA in BAA00327. Ref.2

Sequence conflict

464 – 501

38

DDALW…LSLAS → ARRPVASHKTRHVAKCGSTI SCESVAGGVYAAEVIAGVVN in BAA00327. Ref.2

Secondary structure

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501

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

13 – 24

12

Beta strand

29 – 32

4

Beta strand

34 – 36

3

Helix

41 – 43

3

Helix

53 – 58

6

Helix

61 – 77

17

Turn

79 – 81

3

Beta strand

82 – 90

9

Turn

93 – 95

3

Helix

98 – 109

12

Beta strand

110 – 112

3

Beta strand

115 – 117

3

Beta strand

121 – 124

4

Beta strand

129 – 131

3

Beta strand

137 – 146

10

Helix

148 – 161

14

Beta strand

165 – 167

3

Beta strand

169 – 178

10

Beta strand

181 – 188

8

Turn

189 – 191

3

Beta strand

194 – 200

7

Beta strand

202 – 204

3

Helix

207 – 209

3

Helix

210 – 216

7

Beta strand

229 – 237

9

Beta strand

239 – 241

3

Beta strand

245 – 249

5

Beta strand

255 – 261

7

Turn

262 – 264

3

Beta strand

265 – 269

5

Helix

279 – 281

3

Helix

286 – 299

14

Beta strand

300 – 302

3

Helix

306 – 308

3

Beta strand

311 – 317

7

Helix

327 – 329

3

Beta strand

335 – 341

7

Beta strand

344 – 351

8

Helix

355 – 357

3

Helix

358 – 369

12

Helix

370 – 372

3

Helix

381 – 383

3

Beta 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

Beta strand

495 – 498

4

Sequences

	Sequence		Length	Mass (Da)
	P13035-1 [UniParc]. Last modified May 1, 1992. Version 3. Checksum: 1C4D341E9E4536AB	FASTA	501	56,751
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12." Austin D., Larson T.J. J. Bacteriol. 173:101-107(1991) [PubMed: 1987111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of Escherichia coli and regulation by the cAMP-CRP complex." Choi Y.-L., Kawase S., Kawamukai M., Utsumi R., Sakai H., Komano T. Agric. Biol. Chem. 53:1135-1143(1989) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Structures of the promoter and operator of the glpD gene encoding aerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12." Ye S., Larson T.J. J. Bacteriol. 170:4209-4215(1988) [PubMed: 3045087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61. Strain: K12.
[6]	"Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12." Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M., Utsumi R., Kohara Y., Akiyama K. Nucleic Acids Res. 16:7732-7732(1988) [PubMed: 3045764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M55989 Genomic DNA. Translation: AAA24636.1.
M96795 Genomic DNA. Translation: AAC28164.1.
D00425 Genomic DNA. Translation: BAA00327.1.
U18997 Genomic DNA. Translation: AAA58224.1.
U00096 Genomic DNA. Translation: AAC76451.1.
AP009048 Genomic DNA. Translation: BAE77866.1.
M21277 Genomic DNA. Translation: AAA23885.1.
M54940 Genomic DNA. Translation: AAA23888.1. Different initiation.

PIR

DEECGD. A39186.

RefSeq

AP_004365.1.
NP_417884.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QCU	X-ray	1.75	A/B	1-501	[»]
2R45	X-ray	2.30	A/B	1-501	[»]
2R46	X-ray	2.10	A/B	1-501	[»]
2R4E	X-ray	2.10	A/B	1-501	[»]
2R4J	X-ray	1.96	A/B	1-501	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9793N.

IntAct

P13035. 90 interactions.

2-D gel databases

SWISS-2DPAGE

P13035.

ECO2DBASE

H047.3. 6TH EDITION.

Genome annotation databases

GeneID

947934.

GenomeReviews

Gene locus JW3389 in contig AP009048_GR.
Gene locus b3426 in contig U00096_GR.

KEGG

ecj:JW3389.
eco:b3426.

Organism-specific databases

EchoBASE

EB0389.

EcoGene

EG10394. glpD.

CMR

Search...

Phylogenomic databases

HOGENOM

P13035.

OMA

P13035. LKVYNTH.

Enzyme and pathway databases

BioCyc

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

Family and domain databases

InterPro

IPR000447. FAD-dep_Gly3P_DH.
IPR006076. FAD-dep_OxRdtase.
[Graphical view]

Pfam

PF01266. DAO. 1 hit.
[Graphical view]

PRINTS

PR01001. FADG3PDH.

PROSITE

PS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLPD_ECOLI

Accession

Primary (citable) accession number: P13035
Secondary accession number(s): P78115, Q2M790, Q47234

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)