ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q4MQ58


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name G3P1_BACCE
Primary accession number Q4MQ58
Secondary accession number P83078
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 17)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 1
Synonyms GAPDH 1
EC 1.2.1.12
Gene name
Name: gap1
ORFNames: BCE_G9241_5218
From
Bacillus cereus [TaxID: 1396] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=G9241;
DOI=10.1073/pnas.0402414101; PubMed=15155910 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax.";
Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
[2]
PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
STRAIN=NCIMB 11796 / DSM 626;
DOI=10.1046/j.1365-2672.2001.01478.x; PubMed=11851817 [NCBI, ExPASy, EBI, Israel, Japan]
Browne N., Dowds B.C.A.;
"Heat and salt stress in the food pathogen Bacillus cereus.";
J. Appl. Microbiol. 91:1085-1094(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AAEK01000016; EAL14305.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
SMR Q4MQ58; 3-334.
ModBase Q4MQ58.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS Q4MQ58.
Other
ProtoNet Q4MQ58.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   334  333     Glyceraldehyde-3-phosphate dehydrogenase 1. PRO_0000271247
NP_BIND   11    12  2     NAD (By similarity). 
REGION   150   152  3     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   151   151        Nucleophile (By similarity). 
BINDING   33    33        NAD (By similarity). 
BINDING   77    77        NAD; via carbonyl oxygen (By similarity). 
BINDING   119   119        NAD (By similarity). 
BINDING   181   181        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   196   196        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   232   232        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   314   314        NAD (By similarity). 
SITE   178   178  1     Activates thiol group during catalysis (By similarity). 
CONFLICT   13    13        G -> R (in Ref. 2; AA sequence). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 35826 Da [This is the MW of the unprocessed precursor] CRC64: D5E1F3F4C45BF23B [This is a checksum on the sequence]
        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 

Q4MQ58 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!