KEGG   ENZYME: 3.9.1.3
Entry
EC 3.9.1.3                  Enzyme                                 

Name
phosphohistidine phosphatase;
PHPT1 (gene name);
protein histidine phosphatase;
PHP
Class
Hydrolases;
Acting on phosphorus-nitrogen bonds;
Acting on phosphorus-nitrogen bonds (only sub-subclass identified to date)
Sysname
[protein]-N-phospho-L-histidine phosphohydrolase
Reaction(IUBMB)
a [protein]-N-phospho-L-histidine + H2O = a [protein]-L-histidine + phosphate [RN:R11258 R11259]
Reaction(KEGG)
R11258 R11259
Substrate
[protein]-N-pros-phospho-L-histidine [CPD:C04261];
[protein]-N-tele-phospho-L-histidine [CPD:C04262];
H2O [CPD:C00001]
Product
[protein]-L-histidine [CPD:C00615];
phosphate [CPD:C00009]
Comment
This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides. The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most) [4]. The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein. The enzyme is also active on free phosphoramidate [1,4] and peptide-bound phospholysine [5].
History
EC 3.9.1.3 created 2016
Orthology
K01112  phosphohistidine phosphatase
Genes
HSA: 29085(PHPT1)
PTR: 104008061(PHPT1)
PPS: 100981762(PHPT1)
GGO: 101127423(PHPT1)
PON: 100174576(PHPT1)
NLE: 100605190(PHPT1)
MCC: 721674(PHPT1)
MCF: 102131687(MAMDC4)
CSAB: 103239603(PHPT1)
RRO: 104659598 104669652(PHPT1)
RBB: 108542886(PHPT1)
CJC: 100402534(PHPT1)
SBQ: 101036378(PHPT1)
MMU: 75454(Phpt1)
MCAL: 110289834(Phpt1)
MPAH: 110319198(Phpt1)
RNO: 296571(Phpt1)
MUN: 110557001(Phpt1)
CGE: 100761523(Phpt1)
NGI: 103741191(Phpt1)
HGL: 101705528(Phpt1)
CCAN: 109699335(Phpt1)
TUP: 102485128(PHPT1)
CFA: 491245(PHPT1)
VVP: 112906872(PHPT1)
AML: 100475360(PHPT1)
UMR: 103667072 103675296(PHPT1)
ORO: 101371338(PHPT1)
ELK: 111146033
FCA: 101098343(PHPT1)
PTG: 102966231(PHPT1)
PPAD: 109258803(PHPT1)
AJU: 106989492(PHPT1)
BTA: 618691(PHPT1)
BOM: 102281185(PHPT1)
BIU: 109566628(PHPT1)
BBUB: 102391675(PHPT1) 112582691
CHX: 102185373(PHPT1)
OAS: 101109947(PHPT1)
CFR: 102511170(PHPT1)
CDK: 105106201(PHPT1)
BACU: 103014630(PHPT1)
LVE: 103089622(PHPT1)
OOR: 101282046(PHPT1)
DLE: 111177012(PHPT1)
PCAD: 102979869(PHPT1) 112062758
EPZ: 103567827(PHPT1)
EAI: 106845536(PHPT1)
MYB: 106724000(PHPT1)
MYD: 102771209(PHPT1)
MNA: 107536210(PHPT1)
HAI: 109381651(PHPT1)
DRO: 112306585(PHPT1)
PALE: 102888846(PHPT1)
RAY: 107503115(PHPT1)
MJV: 108406830(PHPT1)
LAV: 100670682(PHPT1)
TMU: 101354410
MDO: 100017116(PHPT1)
SHR: 100934482(PHPT1)
PCW: 110205314(PHPT1)
OAA: 100085648(PHPT1) 114808686
GGA: 424401 770750(PHPT1)
MGP: 100546004(PHPT1) 100548654
CJO: 107317233 107321627(PHPT1)
NMEL: 110402443 110406762(PHPT1)
APLA: 101795226 106015461(PHPT1)
ACYG: 106041604(PHPT1)
TGU: 100189978 100190052(PHPT1)
LSR: 110472220(PHPT1) 110478906
SCAN: 103823377 115484621(PHPT1)
FAB: 101807901(PHPT1) 101808988
PHI: 102106999(PHPT1) 102114133
PMAJ: 107208231 107212113(PHPT1)
CCAE: 111932649(PHPT1)
CCW: 104695463 120410902(PHPT1)
ETL: 114063561 114064156(PHPT1)
CLV: 102094516(PHPT1) 102095723
EGZ: 104135669(PHPT1)
NNI: 104010433
PADL: 103914107(PHPT1)
AAM: 106493878 106494224(PHPT1)
ASN: 102369468(PHPT1) 102376846
AMJ: 102563666(PHPT1) 102574934
PSS: 102447649 102448039(PHPT1)
CMY: 102944694(PHPT1) 119566950
CPIC: 103305695(PHPT1) 103306509
ACS: 100557188 100558315(phpt1)
PVT: 110087442(PHPT1) 110090928
PBI: 103056567(PHPT1)
PMUR: 107302546(PHPT1) 107302839
TSR: 106541992(PHPT1) 106543739
GJA: 107106118 107115168(PHPT1)
XLA: 108714493 734838(phpt1.L)
XTR: 100494164 100497662(phpt1)
NPR: 108787256(PHPT1) 108797455
DRE: 445172(phpt1) 558617(si:dkey-51e6.1)
IPU: 100528926(phpt1) 108257519
PHYP: 113535614(phpt1) 113546801
AMEX: 103037051 103043613(phpt1)
EEE: 113573420(phpt1) 113585141
TRU: 101073866(phpt1) 101075763
NCC: 104952282 104966792(phpt1)
OLA: 101156809 101164173(phpt1)
XMA: 102219858(phpt1) 102237406
XCO: 114149088(phpt1) 114150312
PRET: 103463570(phpt1)
CVG: 107098573 107105104(phpt1)
NFU: 107375130(phpt1) 107393216
KMR: 108230593(si:dkey-51e6.1) 108241411(phpt1)
AOCE: 111571557(phpt1) 111573592
CSEM: 103389195(phpt1) 103397941
POV: 109625906 109640317(phpt1)
SDU: 111232112 111238479(phpt1)
BPEC: 110164001(phpt1) 110167832
MALB: 109964015 109970886(phpt1)
SASA: 106560654(PHP14) 106563239(phpt1) 106565536(PHP14) 106591792
SFM: 108935341 108938490(phpt1)
PKI: 111833403(phpt1) 111840127
LCM: 102349364 102354005(PHPT1)
BFO: 118421611
SPU: 578308
APLC: 110976262
SKO: 100366766
DME: Dmel_CG18662(CG18662) Dmel_CG7929(ocn) Dmel_CG7931(janB) Dmel_CG7933(janA)
DSI: Dsimw501_GD17399(Dsim_janA) Dsimw501_GD17410(Dsim_janB) Dsimw501_GD17421(Dsim_ocn) Dsimw501_GD23579(Dsim_GD23579)
DYA: Dyak_GE18815 Dyak_GE23419(Dyak_janA) Dyak_GE23420(Dyak_janB) Dyak_GE23422(Dyak_ocn)
MDE: 101895156
LCQ: 111675306
AAG: 5564632
AME: 100576467
BTER: 100651751
CCAL: 108628614
OBB: 114873203
SOC: 105201982
MPHA: 105834099
AEC: 105149025
PBAR: 105427733
VEM: 105565463
HST: 105191607
DQU: 106745497
CFO: 105254982
LHU: 105667425
PGC: 109856667
OBO: 105283372
PCF: 106786194
NVI: 103316255
CSOL: 105369036
MDL: 103571115
TCA: 662760
DPA: 109546278
ATD: 109593853
NVL: 108558730
BMOR: 692960
BMAN: 114244039
PRAP: 110994993
HAW: 110380765
TNL: 113496671
API: 100169489
DNX: 107173585
AGS: 114125221
RMD: 113557509
BTAB: 109030869
CLEC: 106661103
ZNE: 110836614
FCD: 110861341
PVM: 113821321
TUT: 107359989
DPTE: 113788759
CSCU: 111633646
PTEP: 107440439
CEL: CELE_F36A2.8(phip-1)
CBR: CBG12374
BMY: Bm1_23000
CRG: 105328285
MYI: 110464427
OBI: 106875271
LAK: 106157674
NVE: 5506033
EPA: 110250310
ADF: 107343753
AMIL: 114961179
PDAM: 113682272
SPIS: 111339461
HMG: 100213884
AQU: 100636166
SMIN: v1.2.015552.t1(symbB.v1.2.015552.t1) v1.2.024049.t1(symbB.v1.2.024049.t1)
 » show all
Reference
1  [PMID:12383260]
  Authors
Ek P, Pettersson G, Ek B, Gong F, Li JP, Zetterqvist O
  Title
Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase.
  Journal
Eur J Biochem 269:5016-23 (2002)
DOI:10.1046/j.1432-1033.2002.03206.x
  Sequence
[hsa:29085]
Reference
2  [PMID:12468887]
  Authors
Klumpp S, Hermesmeier J, Selke D, Baumeister R, Kellner R, Krieglstein J
  Title
Protein histidine phosphatase: a novel enzyme with potency for neuronal signaling.
  Journal
J Cereb Blood Flow Metab 22:1420-4 (2002)
DOI:10.1097/01.wcb.0000045041.03034.99
Reference
3  [PMID:17200567]
  Authors
Baumer N, Maurer A, Krieglstein J, Klumpp S
  Title
Expression of protein histidine phosphatase in Escherichia coli, purification, and determination of enzyme activity.
  Journal
Methods Mol Biol 365:247-60 (2007)
DOI:10.1385/1-59745-267-X:247
Reference
4  [PMID:19836471]
  Authors
Attwood PV, Ludwig K, Bergander K, Besant PG, Adina-Zada A, Krieglstein J, Klumpp S
  Title
Chemical phosphorylation of histidine-containing peptides based on the sequence of histone H4 and their dephosphorylation by protein histidine phosphatase.
  Journal
Biochim Biophys Acta 1804:199-205 (2010)
DOI:10.1016/j.bbapap.2009.10.007
Reference
5  [PMID:25574816]
  Authors
Ek P, Ek B, Zetterqvist O
  Title
Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine.
  Journal
Ups J Med Sci 120:20-7 (2015)
DOI:10.3109/03009734.2014.996720
  Sequence
[hsa:29085]
Other DBs
ExplorEnz - The Enzyme Database: 3.9.1.3
IUBMB Enzyme Nomenclature: 3.9.1.3
ExPASy - ENZYME nomenclature database: 3.9.1.3
BRENDA, the Enzyme Database: 3.9.1.3

DBGET integrated database retrieval system