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Multifunctional virulence effector protein DrrA (Defects in Rab1 recruitment protein A) [Includes: Adenosine monophosphate-protein transferase (AMPylator) (EC 2.7.7.n1) (Guanosine monophosphate-protein transferase) (GMPylator) (EC 2.7.7.n6); Rab1 guanine nucleotide exchange factor]

 DRRA_LEGPH              Reviewed;         647 AA.
Q5ZSQ3;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
16-JAN-2019, entry version 75.
RecName: Full=Multifunctional virulence effector protein DrrA;
AltName: Full=Defects in Rab1 recruitment protein A;
Includes:
RecName: Full=Protein adenylyltransferase;
Short=AMPylator;
EC=2.7.7.n1;
AltName: Full=Protein guanylyltransferase;
Short=GMPylator;
EC=2.7.7.n6;
Includes:
RecName: Full=Rab1 guanine nucleotide exchange factor;
Name=drrA; Synonyms=sidM; OrderedLocusNames=lpg2464;
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 /
ATCC 33152 / DSM 7513).
Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
Legionellaceae; Legionella.
NCBI_TaxID=272624;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS A GUANINE NUCLEOTIDE EXCHANGE
FACTOR, AND SUBCELLULAR LOCATION.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=16824952; DOI=10.1016/j.devcel.2006.05.013;
Machner M.P., Isberg R.R.;
"Targeting of host Rab GTPase function by the intravacuolar pathogen
Legionella pneumophila.";
Dev. Cell 11:47-56(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=15448271; DOI=10.1126/science.1099776;
Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M.,
Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J.,
Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R.,
Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E.,
Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G.,
Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J.,
Ju J., Kalachikov S., Shuman H.A., Russo J.J.;
"The genomic sequence of the accidental pathogen Legionella
pneumophila.";
Science 305:1966-1968(2004).
[3]
FUNCTION.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=17947549; DOI=10.1126/science.1149121;
Machner M.P., Isberg R.R.;
"A bifunctional bacterial protein links GDI displacement to Rab1
activation.";
Science 318:974-977(2007).
[4]
FUNCTION.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=21822290; DOI=10.1038/nature10335;
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
"Modulation of Rab GTPase function by a protein phosphocholine
transferase.";
Nature 477:103-106(2011).
[5]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 340-533, FUNCTION, AND
MUTAGENESIS OF 451-ASN--ARG-453; ASP-480 AND SER-483.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=20064470; DOI=10.1016/j.molcel.2009.11.014;
Schoebel S., Oesterlin L.K., Blankenfeldt W., Goody R.S., Itzen A.;
"RabGDI displacement by DrrA from Legionella is a consequence of its
guanine nucleotide exchange activity.";
Mol. Cell 36:1060-1072(2009).
[6]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 317-533, FUNCTION,
INTERACTION WITH HOST RAB1A, AND MUTAGENESIS OF ALA-435.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=19942850; DOI=10.1038/emboj.2009.347;
Suh H.Y., Lee D.W., Lee K.H., Ku B., Choi S.J., Woo J.S., Kim Y.G.,
Oh B.H.;
"Structural insights into the dual nucleotide exchange and GDI
displacement activity of SidM/DrrA.";
EMBO J. 29:496-504(2010).
[7]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 193-550, FUNCTION,
INTERACTION WITH HOST RAB1A, AND MUTAGENESIS OF TRP-410; GLY-431;
ALA-435; 451-ASN--ARG-453; ARG-541; LYS-568 AND THR-619.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=20176951; DOI=10.1073/pnas.0914231107;
Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F.;
"Structural mechanism of host Rab1 activation by the bifunctional
Legionella type IV effector SidM/DrrA.";
Proc. Natl. Acad. Sci. U.S.A. 107:4699-4704(2010).
[8]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 340-647, AND
PTDINS(4)P-BINDING.
STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
PubMed=20616805; DOI=10.1038/embor.2010.97;
Schoebel S., Blankenfeldt W., Goody R.S., Itzen A.;
"High-affinity binding of phosphatidylinositol 4-phosphate by
Legionella pneumophila DrrA.";
EMBO Rep. 11:598-604(2010).
-!- FUNCTION: Virulence effector that plays a key role in hijacking
the host vesicular trafficking by recruiting the small guanosine
triphosphatase (GTPase) Rab1 to the cytosolic face of the
Legionella-containing vacuole (LCVs). Acts as a GDP-GTP exchange
factor (GEF) for the small GTPase Rab1 (RAB1A, RAB1B or RAB1C),
thereby converting Rab1 to an active GTP-bound state, leading to
the incorporation of Rab1 into LCVs. Also shows RabGDI
displacement factor (GDF) activity; however, this probably
represents a passive activity following the GEF activity. Also
acts as an adenylyltransferase by mediating the addition of
adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B,
thereby rendering RAB1B constitutively active. Also has
adenylyltransferase activity towards Rab6 and Rab35. Also displays
guanylyltransferase activity by mediating the addition of
guanosine 5'-monophosphate (GMP) to host RAB1B in vitro; however
such activity remains uncertain in vivo. Specifically binds
phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the
cytosolic surface of the phagosomal membrane shortly after
infection. {ECO:0000269|PubMed:16824952,
ECO:0000269|PubMed:17947549, ECO:0000269|PubMed:19942850,
ECO:0000269|PubMed:20064470, ECO:0000269|PubMed:20176951,
ECO:0000269|PubMed:21822290}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-
adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-
COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624;
EC=2.7.7.n1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-
threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292,
Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113;
EC=2.7.7.n1;
-!- CATALYTIC ACTIVITY:
Reaction=GTP + L-tyrosyl-[protein] = diphosphate + O-(5'-
guanylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54296, Rhea:RHEA-
COMP:10136, Rhea:RHEA-COMP:13848, ChEBI:CHEBI:33019,
ChEBI:CHEBI:37565, ChEBI:CHEBI:46858, ChEBI:CHEBI:138114;
EC=2.7.7.n6;
-!- SUBUNIT: Interacts with host RAB1A. {ECO:0000269|PubMed:19942850,
ECO:0000269|PubMed:20176951}.
-!- INTERACTION:
P62820:RAB1A (xeno); NbExp=7; IntAct=EBI-7632432, EBI-716845;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16824952}. Host
cytoplasmic vesicle membrane {ECO:0000269|PubMed:16824952};
Peripheral membrane protein {ECO:0000269|PubMed:16824952}.
Note=Translocated into the host cell via the type IV secretion
system (T4SS). Membrane association is mediated by PtdIns(4)P-
binding.
-!- DOMAIN: The P4M (PtdIns(4)P-binding) region mediates binding to
PtdIns(4)P and membrane attachment. {ECO:0000250}.
-!- SIMILARITY: Belongs to the DrrA family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; DQ845395; ABG90503.1; -; mRNA.
EMBL; AE017354; AAU28524.1; -; Genomic_DNA.
RefSeq; WP_010948166.1; NC_002942.5.
RefSeq; YP_096471.1; NC_002942.5.
PDB; 2WWX; X-ray; 1.50 A; B=317-533.
PDB; 3JZ9; X-ray; 1.80 A; A=340-533.
PDB; 3JZA; X-ray; 1.80 A; B=340-533.
PDB; 3L0I; X-ray; 2.85 A; A/C=193-550.
PDB; 3L0M; X-ray; 3.45 A; A/B=317-647.
PDB; 3N6O; X-ray; 2.50 A; A/B=340-647.
PDB; 4MXP; X-ray; 1.83 A; A=330-647.
PDBsum; 2WWX; -.
PDBsum; 3JZ9; -.
PDBsum; 3JZA; -.
PDBsum; 3L0I; -.
PDBsum; 3L0M; -.
PDBsum; 3N6O; -.
PDBsum; 4MXP; -.
SMR; Q5ZSQ3; -.
IntAct; Q5ZSQ3; 1.
MINT; Q5ZSQ3; -.
STRING; 272624.lpg2464; -.
PaxDb; Q5ZSQ3; -.
PRIDE; Q5ZSQ3; -.
EnsemblBacteria; AAU28524; AAU28524; lpg2464.
GeneID; 19834029; -.
KEGG; lpn:lpg2464; -.
PATRIC; fig|272624.6.peg.2613; -.
HOGENOM; HOG000126893; -.
KO; K15480; -.
OMA; AQATEYS; -.
EvolutionaryTrace; Q5ZSQ3; -.
Proteomes; UP000000609; Chromosome.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044161; C:host cell cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0044600; F:protein guanylyltransferase activity; ISS:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
GO; GO:0009405; P:pathogenesis; ISS:UniProtKB.
GO; GO:0018117; P:protein adenylylation; ISS:UniProtKB.
GO; GO:0018260; P:protein guanylylation; ISS:UniProtKB.
GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
CDD; cd11689; SidM_DrrA_GEF; 1.
Gene3D; 1.20.1280.280; -; 1.
InterPro; IPR033784; DrrA_GEF.
InterPro; IPR028057; DrrA_P4M.
InterPro; IPR038346; DrrA_PI4P-bd_sf.
Pfam; PF14860; DrrA_P4M; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome;
Guanine-nucleotide releasing factor; Host cytoplasmic vesicle;
Host membrane; Lipid-binding; Membrane; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
Secreted; Transferase; Virulence.
CHAIN 1 647 Multifunctional virulence effector
protein DrrA.
/FTId=PRO_0000417545.
REGION 1 339 Protein
adenylyltransferase/guanylyltransferase.
REGION 340 520 Rab1 guanine nucleotide exchange factor.
REGION 544 647 P4M region.
MUTAGEN 410 410 W->D: Almost abolishes GEF and GDF
activities, but still binds Rab1.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 431 431 G->D: Abolishes GEF and GDF activities,
but still binds Rab1.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 435 435 A->D,E: Abolishes GEF and GDF activities,
but still binds Rab1.
{ECO:0000269|PubMed:19942850,
ECO:0000269|PubMed:20176951}.
MUTAGEN 451 453 NER->AEA: Almost abolishes GEF and GDF
activities, with a more severe effect on
GEF activity.
{ECO:0000269|PubMed:20064470,
ECO:0000269|PubMed:20176951}.
MUTAGEN 480 480 D->A: Slightly impairs GEF and GDF
activities; when associated with A-483.
{ECO:0000269|PubMed:20064470}.
MUTAGEN 483 483 S->A: Slightly impairs GEF and GDF
activities; when associated with A-480.
{ECO:0000269|PubMed:20064470}.
MUTAGEN 541 541 R->A: Abolishes PtdIns(4)P-binding; when
associated with A-568.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 568 568 K->A: Abolishes PtdIns(4)P-binding; when
associated with A-541 or A-619.
{ECO:0000269|PubMed:20176951}.
MUTAGEN 619 619 T->A: Abolishes PtdIns(4)P-binding; when
associated with A-568.
{ECO:0000269|PubMed:20176951}.
HELIX 214 224 {ECO:0000244|PDB:3L0I}.
HELIX 240 243 {ECO:0000244|PDB:3L0I}.
HELIX 245 258 {ECO:0000244|PDB:3L0I}.
HELIX 271 280 {ECO:0000244|PDB:3L0I}.
HELIX 286 307 {ECO:0000244|PDB:3L0I}.
HELIX 320 322 {ECO:0000244|PDB:3L0I}.
HELIX 336 361 {ECO:0000244|PDB:2WWX}.
HELIX 365 381 {ECO:0000244|PDB:2WWX}.
HELIX 386 389 {ECO:0000244|PDB:2WWX}.
HELIX 390 393 {ECO:0000244|PDB:2WWX}.
HELIX 400 419 {ECO:0000244|PDB:2WWX}.
HELIX 428 447 {ECO:0000244|PDB:2WWX}.
STRAND 450 452 {ECO:0000244|PDB:3JZ9}.
HELIX 458 460 {ECO:0000244|PDB:3JZA}.
HELIX 464 478 {ECO:0000244|PDB:2WWX}.
HELIX 490 506 {ECO:0000244|PDB:2WWX}.
HELIX 512 520 {ECO:0000244|PDB:2WWX}.
STRAND 526 528 {ECO:0000244|PDB:3JZ9}.
TURN 530 533 {ECO:0000244|PDB:3L0I}.
HELIX 557 559 {ECO:0000244|PDB:4MXP}.
HELIX 564 579 {ECO:0000244|PDB:4MXP}.
HELIX 585 596 {ECO:0000244|PDB:4MXP}.
HELIX 599 605 {ECO:0000244|PDB:4MXP}.
HELIX 610 615 {ECO:0000244|PDB:4MXP}.
HELIX 620 645 {ECO:0000244|PDB:4MXP}.
SEQUENCE 647 AA; 73422 MW; DCE6EC98BCC3CDCA CRC64;
MSIMGRIKMS VNEEQFGSLY SDERDKPLLS PTAQKKFEEY QNKLANLSKI IRENEGNEVS
PWQEWENGLR QIYKEMIYDA FDALGVEMPK DMEVHFAGSL AKAQATEYSD LDAFVIVKND
EDIKKVKPVF DALNNLCQRI FTASNQIYPD PIGINPSRLI GTPDDLFGML KDGMVADVEA
TAMSILTSKP VLPRYELGEE LRDKIKQEPS FSNMVSAKKF YNKAIKDFTA PKEGAEVVSV
KTHIMRPIDF MLMGLREEFN LYSEDGAHLS APGTIRLLRE KNLLPEEQIA RIESVYNQAM
SKRFELHAEH KKEHDEMPYS DAKAMLDEVA KIRELGVQRV TRIENLENAK KLWDNANSML
EKGNISGYLK AANELHKFMK EKNLKEDDLR PELSDKTISP KGYAILQSLW GAASDYSRAA
ATLTESTVEP GLVSAVNKMS AFFMDCKLSP NERATPDPDF KVGKSKILVG IMQFIKDVAD
PTSKIWMHNT KALMNHKIAA IQKLERSNNV NDETLESVLS SKGENLSEYL SYKYATKDEG
REHRYTASTE NFKNVKEKYQ QMRGDALKTE ILADFKDKLA EATDEQSLKQ IVAELKSKDE
YRILAKGQGL TTQLLGLKTS SVSSFEKMVE ETRESIKSQE RQTIKIK


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Pathways :
WP1714: Tyrosine metabolism
WP2292: Chemokine signaling pathway
WP1678: Nucleotide excision repair
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[drrA sidM lpg2464] Multifunctional virulence effector protein DrrA (Defects in Rab1 recruitment protein A) [Includes: Protein adenylyltransferase (AMPylator) (EC 2.7.7.n1) (Protein guanylyltransferase) (GMPylator) (EC 2.7.7.n6); Rab1 guanine nucleotide exchange factor]
[drrA sidM] Multifunctional virulence effector protein DrrA (Defects in Rab1 recruitment protein A) [Includes: Protein adenylyltransferase (AMPylator) (EC 2.7.7.n1) (Protein guanylyltransferase) (GMPylator) (EC 2.7.7.n6); Rab1 guanine nucleotide exchange factor]
[RAB1B] Ras-related protein Rab-1B
[RAB1A RAB1] Ras-related protein Rab-1A
[FTO KIAA1752] Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-)
[Fto Kiaa1752] Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (Protein fatso) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-)
[Fto] Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-)
[FTO] Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-)
[Rab1b] Ras-related protein Rab-1B
[Alkbh1 Abh Alkbh] Nucleic acid dioxygenase ALKBH1 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 1) (Alpha-ketoglutarate-dependent dioxygenase ABH1) (DNA 6mA demethylase) (DNA N6-methyl adenine demethylase) (EC 1.14.11.51) (DNA lyase ABH1) (EC 4.2.99.18) (DNA oxidative demethylase ALKBH1) (EC 1.14.11.33) (tRNA N1-methyl adenine demethylase) (EC 1.14.11.-)
[ALKBH1 ABH ABH1 ALKBH] Nucleic acid dioxygenase ALKBH1 (EC 1.14.11.-) (Alkylated DNA repair protein alkB homolog 1) (Alpha-ketoglutarate-dependent dioxygenase ABH1) (DNA 6mA demethylase) (DNA N6-methyl adenine demethylase) (EC 1.14.11.51) (DNA lyase ABH1) (EC 4.2.99.18) (DNA oxidative demethylase ALKBH1) (EC 1.14.11.33) (tRNA N1-methyl adenine demethylase) (EC 1.14.11.-)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Mettl3 Mta70] N6-adenosine-methyltransferase subunit METTL3 (EC 2.1.1.348) (Methyltransferase-like protein 3) (N6-adenosine-methyltransferase 70 kDa subunit) (MT-A70)
[TRMT10C MRPP1 RG9MTD1] tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)
[Mettl16 Mett10d] RNA N6-adenosine-methyltransferase METTL16 (Methyltransferase 10 domain-containing protein) (Methyltransferase-like protein 16) (N6-adenosine-methyltransferase METTL16) (EC 2.1.1.348) (U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase) (EC 2.1.1.346)
[METTL16 METT10D] RNA N6-adenosine-methyltransferase METTL16 (Methyltransferase 10 domain-containing protein) (Methyltransferase-like protein 16) (N6-adenosine-methyltransferase METTL16) (EC 2.1.1.348) (U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase) (EC 2.1.1.346)
[METTL3 MTA70] N6-adenosine-methyltransferase catalytic subunit (EC 2.1.1.348) (Methyltransferase-like protein 3) (hMETTL3) (N6-adenosine-methyltransferase 70 kDa subunit) (MT-A70)
[tsaD gcp ygjD b3064 JW3036] tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD) (tRNA threonylcarbamoyladenosine biosynthesis protein TsaD)
[hchA ECH7EC869_3386] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[TRMT10C MRPP1 RG9MTD1] tRNA methyltransferase 10 homolog C (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221)
[GBF1 KIAA0248] Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (BFA-resistant GEF 1)
[ibpA p76 HSM_1489] Protein adenylyltransferase and cysteine protease IbpA (HMW IgBP) (p120) [Cleaved into: Protein p76 IgBP (76 kDa antigen)] [Includes: Protein adenylyltransferase IbpA (EC 2.7.7.n1) (AMPylator IbpA); Cysteine protease IbpA (EC 3.4.22.-)]
[hchA ECH74115_2746] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[HACE1 KIAA1320] E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1)
[] Guanine nucleotide exchange C9orf72 homolog
[sdeA lpg2157] Ubiquitinating/deubiquitinating enzyme SdeA (Effector protein SdeA) [Includes: Deubiquitinase (DUB) (EC 3.4.22.-) (Deneddylase) (Deubiquitinating enzyme); Ubiquitin transferase (EC 2.3.2.-); Mono-ADP-ribosyltransferase (mART) (EC 2.4.2.31)]
[C9orf72] Guanine nucleotide exchange C9orf72
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[PARK7] Protein/nucleic acid deglycase DJ-1 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) (Oncogene DJ1) (Parkinson disease protein 7) (Parkinsonism-associated deglycase) (Protein DJ-1) (DJ-1)

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