Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q4MQ58 (G3P1_BACCE)

Last modified November 25, 2008. Version 19. 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

Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 1
      Short name=GAPDH 1
    EC=1.2.1.12
Gene names
Name: gap1
ORF Names: BCE_G9241_5218
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subcellular location

Cytoplasm.

Induction

Repressed by salt stress.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect 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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 334333Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000271247

Regions

Nucleotide binding11 – 122NAD By similarity
Region150 – 1523Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1511Nucleophile By similarity
Binding site331NAD By similarity
Binding site771NAD; via carbonyl oxygen By similarity
Binding site1191NAD By similarity
Binding site1811Glyceraldehyde 3-phosphate By similarity
Binding site1961Glyceraldehyde 3-phosphate By similarity
Binding site2321Glyceraldehyde 3-phosphate By similarity
Binding site3141NAD By similarity
Site1781Activates thiol group during catalysis By similarity

Experimental info

Sequence conflict131G → R AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q4MQ58-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D5E1F3F4C45BF23B

FASTA33435,826
        10         20         30         40         50         60 
MTKIGINGFG RIGRNVFRAA LNNSEVEVVA INDLTDAKTL AHLLKYDTVH GTLNAEVSAN 

        70         80         90        100        110        120 
ENSIVVNGKE IKVIAERDPA QLPWSDYGVE VVVESTGRFT KKSDAEKHLG GSVKKVIISA 

       130        140        150        160        170        180 
PASDEDITVV MGVNHEQYDA ANHNVVSNAS CTTNCLAPFA KVLNEKFGVK RGMMTTIHSY 

       190        200        210        220        230        240 
TNDQQILDLP HKDLRRARAA AENMIPTSTG AAKAVALVLP ELKGKLNGGA VRVPTANVSL 

       250        260        270        280        290        300 
VDLVVELDKE VTVEEVNAAF KAAAEGELKG ILGYSEEPLV SIDYNGCTAS STIDALSTMV 

       310        320        330 
MEGNMVKVLS WYDNETGYSN RVVDLAAYMT SKGL 

« Hide

References

[1]"Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax."
Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., Peterson S.N., Weyant R.S. expand/collapse author list , Galloway D.R., Read T.D., Popovic T., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004) [PubMed: 15155910] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G9241.
[2]"Heat and salt stress in the food pathogen Bacillus cereus."
Browne N., Dowds B.C.A.
J. Appl. Microbiol. 91:1085-1094(2001) [PubMed: 11851817] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, INDUCTION.
Strain: NCIMB 11796 / DSM 626.

Cross-references

Sequence databases

AAEK01000016 Genomic DNA. Translation: EAL14305.1.

3D structure databases

SMRQ4MQ58. Positions 3-334.
ModBaseSearch...

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_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...

Entry information

Entry nameG3P1_BACCE
AccessionPrimary (citable) accession number: Q4MQ58
Secondary accession number(s): P83078
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 19 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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