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Reviewed, UniProtKB/Swiss-Prot P09124 (G3P1_BACSU)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1
    EC=1.2.1.12
Alternative name(s):
    NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
      Short name=GAPDH
Gene names
Name: gapA
Synonyms: gap
Ordered Locus Names: BSU33940
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

More active in catabolism.

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.

Subcellular location

Cytoplasm. Ref.4

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
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 (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.3
Chain2 – 335334Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145634

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 site341NAD 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

Experimental info

Sequence conflict51V → VI AA sequence Ref.4

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Sequences

Sequence LengthMass (Da)Tools
P09124-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B7A422A5CE3AD1DF

FASTA33535,833
        10         20         30         40         50         60 
MAVKVGINGF GRIGRNVFRA ALNNPEVEVV AVNDLTDANM LAHLLQYDSV HGKLDAEVSV 

        70         80         90        100        110        120 
DGNNLVVNGK TIEVSAERDP AKLSWGKQGV EIVVESTGFF TKRADAAKHL EAGAKKVIIS 

       130        140        150        160        170        180 
APANEEDITI VMGVNEDKYD AANHDVISNA SCTTNCLAPF AKVLNDKFGI KRGMMTTVHS 

       190        200        210        220        230        240 
YTNDQQILDL PHKDYRRARA AAENIIPTST GAAKAVSLVL PELKGKLNGG AMRVPTPNVS 

       250        260        270        280        290        300 
LVDLVAELNQ EVTAEEVNAA LKEAAEGDLK GILGYSEEPL VSGDYNGNKN SSTIDALSTM 

       310        320        330 
VMEGSMVKVI SWYDNESGYS NRVVDLAAYI AKKGL

« Hide

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References

« Hide 'large scale' references
[1]"Sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from Bacillus subtilis."
Viaene A., Dhaese P.
Nucleic Acids Res. 17:1251-1251(1989) [PubMed: 2493629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / BD170.
[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]"Cold shock stress-induced proteins in Bacillus subtilis."
Graumann P., Schroeder K., Schmid R., Marahiel M.A.
J. Bacteriol. 178:4611-4619(1996) [PubMed: 8755892] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.
Strain: 168 / JH642.
[4]"Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
Microbiology 146:65-75(2000) [PubMed: 10658653] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12, SUBCELLULAR LOCATION.
Strain: 168.
[5]"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

X13011 Genomic DNA. Translation: CAA31434.1.
AL009126 Genomic DNA. Translation: CAB15399.1.
PIRDEBSG. S02754.
RefSeqNP_391274.1.

3D structure databases

HSSPHSSP built from PDB template 1NQO based on UniProtKB P00362.
SMRP09124. Positions 2-335.
ModBaseSearch...

PTM databases

PhosSiteP09124.

Genome annotation databases

GeneID938627.
GenomeReviewsGene locus BSU33940 in contig AL009126_GR.
KEGGbsu:BSU33940.
NMPDRfig|224308.1.peg.3400.

Organism-specific databases

SubtiListBG10827. gapA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP09124.
OMAP09124. YDSTFGV.

Enzyme and pathway databases

BioCycBSUB224308:BSU3391-MON.
BRENDA1.2.1.12. 150.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]
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 nameG3P1_BACSU
AccessionPrimary (citable) accession number: P09124
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 86 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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