Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A9C1 (GLPA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anaerobic glycerol-3-phosphate dehydrogenase subunit A

Short name=G-3-P dehydrogenase
EC=1.1.5.3
Gene names
Name:glpA
Ordered Locus Names:Z3499, ECs3126
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor By similarity.

Catalytic activity

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.

Cofactor

FAD By similarity.

FMN By similarity.

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.

Subunit structure

Composed of a catalytic GlpA/B dimer and of membrane bound GlpC By similarity.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity. Note: Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase By similarity.

Sequence similarities

Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Anaerobic glycerol-3-phosphate dehydrogenase subunit A
PRO_0000126094

Regions

Nucleotide binding10 – 3829FAD Potential

Sequences

Sequence LengthMass (Da)Tools
P0A9C1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: E5C803F89E912E0E

FASTA54258,958
        10         20         30         40         50         60 
MKTRDSQSSD VIIIGGGATG AGIARDCALR GLRVILVERH DIATGATGRN HGLLHSGARY 

        70         80         90        100        110        120 
AVTDAESARE CISENQILKR IARHCVEPTN GLFITLPEDD LSFQATFIRA CEEAGISAEA 

       130        140        150        160        170        180 
IDPQQARIIE PAVNPALIGA VKVPDGTVDP FRLTAANMLD AKEHGAVILT AHEVTGLIRE 

       190        200        210        220        230        240 
GATVCGVRVR NHLTGETQAL HAPVVVNAAG IWGQHIAEYA DLRIRMFPAK GSLLIMDHRI 

       250        260        270        280        290        300 
NQHVINRCRK PSDADILVPG DTISLIGTTS LRIDYNEIDD NRVTAEEVDI LLREGEKLAP 

       310        320        330        340        350        360 
VMAKTRILRA YSGVRPLVAS DDDPSGRNVS RGIVLLDHAE RDGLDGFITI TGGKLMTYRL 

       370        380        390        400        410        420 
MAEWATDAVC RKLGNTRPCT TADLALPGSQ EPAEVTLRKV ISLPAPLRGS AVYRHGDRTP 

       430        440        450        460        470        480 
AWLSEGRLHR SLVCECEAVT AGEVQYAVEN LNVNSLLDLR RRTRVGMGTC QGELCACRAA 

       490        500        510        520        530        540 
GLLQRFNVTT SAQSIEQLST FLNERWKGVQ PIAWGDALRE SEFTRWVYQG LCGLEKEQKD 


AL 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG57372.1.
BA000007 Genomic DNA. Translation: BAB36549.1.
PIRF91019.
RefSeqNP_288817.1. NC_002655.2.
NP_311153.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A9C1.
SMRP0A9C1. Positions 5-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z3499.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57372; AAG57372; Z3499.
BAB36549; BAB36549; BAB36549.
GeneID916834.
959442.
KEGGece:Z3499.
ecs:ECs3126.
PATRIC18355636. VBIEscCol44059_3019.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0578.
HOGENOMHOG000004814.
KOK00111.
OMAQIDNMEV.
OrthoDBEOG651SR7.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3078-MONOMER.
ECOO157:GLPA-MONOMER.
UniPathwayUPA00618; UER00673.

Family and domain databases

InterProIPR007419. BFD-like_2Fe2S-bd_dom.
IPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
IPR017752. G3P_DH_GlpA_su.
[Graphical view]
PfamPF01266. DAO. 1 hit.
PF04324. Fer2_BFD. 1 hit.
[Graphical view]
PRINTSPR01001. FADG3PDH.
TIGRFAMsTIGR03377. glycerol3P_GlpA. 1 hit.
PROSITEPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLPA_ECO57
AccessionPrimary (citable) accession number: P0A9C1
Secondary accession number(s): P13032, P78238
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 11, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways