Q4MQ58 (G3P1_BACCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase 1
Short name=GAPDH 1
EC=1.2.1.12

Gene names

Name:	gap1
ORF Names:	BCE_G9241_5218

Organism

Bacillus cereus

Taxonomic identifier

1396 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.2
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 334	333	Glyceraldehyde-3-phosphate dehydrogenase 1		PRO_0000271247
Regions
	Nucleotide binding	11 – 12	2	NAD By similarity
	Region	150 – 152	3	Glyceraldehyde 3-phosphate binding By similarity UniProtKB P00362
Sites
	Active site	151	1	Nucleophile By similarity UniProtKB P00362
	Binding site	33	1	NAD By similarity UniProtKB P00362
	Binding site	77	1	NAD; via carbonyl oxygen By similarity UniProtKB P00362
	Binding site	119	1	NAD By similarity UniProtKB P00362
	Binding site	181	1	Glyceraldehyde 3-phosphate By similarity UniProtKB P00362
	Binding site	196	1	Glyceraldehyde 3-phosphate By similarity UniProtKB P00362
	Binding site	232	1	Glyceraldehyde 3-phosphate By similarity UniProtKB P00362
	Binding site	314	1	NAD By similarity UniProtKB P00362
	Site	178	1	Activates thiol group during catalysis By similarity UniProtKB P00362
Experimental info
	Sequence conflict	13	1	G → R AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q4MQ58 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D5E1F3F4C45BF23B	FASTA	334	35,826
	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

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. , 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
EMBL GenBank DDBJ	AAEK01000016 Genomic DNA. Translation: EAL14305.1.
3D structure databases
HSSP	HSSP built from PDB template 1NQO based on UniProtKB P00362.
ProteinModelPortal	Q4MQ58.
SMR	Q4MQ58. Positions 3-334.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	24957964. VBIBacCer116370_2912.
Family and domain databases
InterPro	IPR020831. 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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR10836. GAP_DH. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P1_BACCE

Accession

Primary (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:	January 25, 2012
This is version 38 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program