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Reviewed, UniProtKB/Swiss-Prot O34425 (G3P2_BACSU)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
    EC=1.2.1.59
Alternative name(s):
    NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
      Short name=GAPDH
Gene names
Name: gapB
Ordered Locus Names: BSU29020
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

More active in anabolism.

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

biophysicochemical properties

Kinetic parameters:

The catalytic efficiency is 50-fold higher with NADP than with NAD.

KM=5.7 mM for NAD

KM=0.86 mM for NADP

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from electronic annotation. Source: EC

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145635

Regions

Nucleotide binding12 – 132NAD By similarity
Region151 – 1533Glyceraldehyde 3-phosphate binding By similarity
Region210 – 2112Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1521Nucleophile By similarity
Binding site781NAD; via carbonyl oxygen By similarity
Binding site1821Glyceraldehyde 3-phosphate By similarity
Binding site1971Glyceraldehyde 3-phosphate By similarity
Binding site2331Glyceraldehyde 3-phosphate By similarity
Binding site3151NAD By similarity
Site1791Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
O34425-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DD1DD4BC7D633EC6

FASTA34037,476
        10         20         30         40         50         60 
MKVKVAINGF GRIGRMVFRK AMLDDQIQVV AINASYSAET LAHLIKYDTI HGRYDKEVVA 

        70         80         90        100        110        120 
GEDSLIVNGK KVLLLNSRDP KQLPWREYDI DIVVEATGKF NAKDKAMGHI EAGAKKVILT 

       130        140        150        160        170        180 
APGKNEDVTI VMGVNEDQFD AERHVIISNA SCTTNCLAPV VKVLDEEFGI ESGLMTTVHA 

       190        200        210        220        230        240 
YTNDQKNIDN PHKDLRRARA CGESIIPTTT GAAKALSLVL PHLKGKLHGL ALRVPVPNVS 

       250        260        270        280        290        300 
LVDLVVDLKT DVTAEEVNEA FKRAAKTSMY GVLDYSDEPL VSTDYNTNPH SAVIDGLTTM 

       310        320        330        340 
VMEDRKVKVL AWYDNEWGYS CRVVDLIRHV AARMKHPSAV

« Hide

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References

« Hide 'large scale' references
[1]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium."
Fillinger S., Boschi-Muller S., Azza S., Dervyn E., Branlant G., Aymerich S.
J. Biol. Chem. 275:14031-14037(2000) [PubMed: 10799476] [Abstract]
Cited for: CHARACTERIZATION.

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Cross-references

Sequence databases

AF008220 Genomic DNA. Translation: AAC00355.1.
AL009126 Genomic DNA. Translation: CAB14862.1.
PIRG69628.
RefSeqNP_390780.1.

3D structure databases

HSSPHSSP built from PDB template 1NQO based on UniProtKB P00362.
ModBaseSearch...

Genome annotation databases

GeneID937393.
GenomeReviewsGene locus BSU29020 in contig AL009126_GR.
KEGGbsu:BSU29020.
NMPDRfig|224308.1.peg.2905.

Organism-specific databases

SubtiListBG12592. gapB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO34425.
OMAO34425. TNPHSAI.

Enzyme and pathway databases

BioCycBSUB224308:BSU2898-MON.
BRENDA1.2.1.59. 150.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
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.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3P2_BACSU
AccessionPrimary (citable) accession number: O34425
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents