Skip Header

Contribute Send feedback
Read comments (?) or add your own

P46795 (G3P_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Glyceraldehyde-3-phosphate dehydrogenase

Short name=GAPDH
EC=1.2.1.12
Gene names
Name:gap
Ordered Locus Names:BB_0057
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145636

Regions

Nucleotide binding10 – 112NAD By similarity
Region152 – 1543Glyceraldehyde 3-phosphate binding By similarity
Region211 – 2122Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1531Nucleophile By similarity
Binding site311NAD By similarity
Binding site751NAD; via carbonyl oxygen By similarity
Binding site1831Glyceraldehyde 3-phosphate By similarity
Binding site1981Glyceraldehyde 3-phosphate By similarity
Binding site2341Glyceraldehyde 3-phosphate By similarity
Binding site3181NAD By similarity
Site1801Activates thiol group during catalysis By similarity

Experimental info

Sequence conflict2141A → P in AAB53930. Ref.1
Sequence conflict2941S → P in AAB53930. Ref.1

Secondary structure

.......................................................... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46795 [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: 30E94F98839819C0

FASTA33536,255
        10         20         30         40         50         60 
MKLAINGFGR IGRNVFKIAF ERGIDIVAIN DLTDPKTLAH LLKYDSTFGV YNKKVESRDG 

        70         80         90        100        110        120 
AIVVDGREIK IIAERDPKNL PWAKLGIDVV IESTGVFSSA TSDKGGYLDH VNHAGAKKVI 

       130        140        150        160        170        180 
LTVPAKDEIK TIVLGVNDHD INSDLKAVSN ASCTTNCLAP LAKVLHESFG IEQGLMTTVH 

       190        200        210        220        230        240 
AYTNDQRILD LPHSDLRRAR AAALSIIPTS TGAAKAVGLV LPELKGKLNG TSMRVPVPTG 

       250        260        270        280        290        300 
SIVDLTVQLK KKDVTKEEIN SVLRKASETP ELKGILGYTE DPIVSSDIKG NSHSSIVDGL 

       310        320        330 
ETMVLENGFA KILSWYDNEF GYSTRVVDLA QKLVK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28760 Genomic DNA. Translation: AAB53930.1.
AE000783 Genomic DNA. Translation: AAC66450.1.
PIRA70107.
RefSeqNP_212191.1. NC_001318.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HJAX-ray2.20A/B/C/D1-335[»]
ProteinModelPortalP46795.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000008599; EBBORP00000007929; EBBORG00000008598.
GeneID1194893.
GenomeReviewsGene locus BB_0057 in contig AE000783_GR.
KEGGbbu:BB0057.
NMPDRfig|224326.1.peg.441.
PATRIC20556719. VBIBorBur75917_0455.
TIGRBB_0057.

Phylogenomic databases

GeneTreeEBGT00050000007066.
HOGENOMHBG571736.
OMAEHEITSD.
PhylomeDBP46795.
ProtClustDBCLSK507322.

Enzyme and pathway databases

BioCycBBUR224326:BB_0057-MONOMER.

Family and domain databases

InterProIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00134.
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P_BORBU
AccessionPrimary (citable) accession number: P46795
Secondary accession number(s): O51084
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 15, 1998
Last modified: January 25, 2012
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

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