Aerobic glycerol-3-phosphate dehydrogenase - Escherichia coli (strain K12)

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P13035 (GLPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
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.
Sequence caution	The sequence AAA23888.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glycerol metabolism
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycerol catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glycerol-3-phosphate catabolic process Inferred from mutant phenotype PubMed 5321485. Source: EcoCyc
Cellular_component	glycerol-3-phosphate dehydrogenase complex Inferred from direct assay PubMed 18296637. Source: EcoCyc integral to plasma membrane Inferred from direct assay PubMed 340460. Source: EcoCyc
Molecular_function	electron carrier activity Inferred from direct assay PubMed 340460. Source: EcoCyc sn-glycerol-3-phosphate:ubiquinone oxidoreductase activity Inferred from direct assay PubMed 340460. Source: EcoCyc sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
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

FAD Potential

Experimental info

Sequence conflict

A → G in BAA00327. Ref.2

Sequence conflict

328 – 353

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

Sequence conflict

464 – 501

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

Secondary structure

501

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P13035 [UniParc].

Last modified May 1, 1992. Version 3.
Checksum: 1C4D341E9E4536AB
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
[7]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_417884.1. NC_000913.2.
YP_492007.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P13035.

SMR

P13035. Positions 1-501.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9793N.

IntAct

P13035. 90 interactions.

MINT

MINT-1248675.

STRING

511145.b3426.

2D gel databases

SWISS-2DPAGE

P13035.

Proteomic databases

PaxDb

P13035.

PRIDE

P13035.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76451; AAC76451; b3426.
BAE77866; BAE77866; BAE77866.

GeneID

12932271.
947934.

KEGG

ecj:Y75_p3751.
eco:b3426.

PATRIC

32122288. VBIEscCol129921_3521.

Organism-specific databases

EchoBASE

EB0389.

EcoGene

EG10394. glpD.

Phylogenomic databases

eggNOG

COG0578.

HOGENOM

HOG000004811.

K00111.

OMA

NAEQQSR.

ProtClustDB

PRK12266.

Enzyme and pathway databases

BioCyc

EcoCyc:AERGLYC3PDEHYDROG-MONOMER.
ECOL316407:JW3389-MONOMER.
MetaCyc:AERGLYC3PDEHYDROG-MONOMER.

UniPathway

UPA00618; UER00674.

Gene expression databases

Genevestigator

P13035.

Family and domain databases

InterPro

IPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[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...

Other

EvolutionaryTrace

P13035.

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:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents