HAMAP

Accession	MF_01220
Dates	13-AUG-2002 (Created) 5-JAN-2012 (Last updated, Version 19)

Data class

Protein

Predictors

HAMAP; MF_01220_B; [distribution of match scores in UniProtKB];[seed alignment for MF_01220_B]

Predictors

HAMAP; MF_01220_A; [distribution of match scores in UniProtKB];[seed alignment for MF_01220_A]

Names

PyrH

Identifier

PYRH

Protein name

RecName: Full=Uridylate kinase; Short=UK; EC=2.7.4.22; AltName: Full=Uridine monophosphate kinase; Short=UMP kinase; Short=UMPK;

Gene name

pyrH

FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP (By similarity).

CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP.

ENZYME REGULATION: Allosterically activated by GTP. Inhibited by UTP (By similarity).

ENZYME REGULATION: Inhibited by UTP (By similarity).

PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.

SUBUNIT: Homohexamer (By similarity).

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

SIMILARITY: Belongs to the UMP kinase family.

Pfam	PF00696; AA_kinase; 1;
TIGRFAMs	TIGR02075; PyrH_bact; 1; TIGR02076; PyrH_arch; 1;

Allosteric enzyme.

ATP-binding, Cytoplasm, Kinase, Nucleotide-binding, Pyrimidine biosynthesis, Transferase.

GO:0009041; Molecular function: uridylate kinase activity.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.

From: PYRH_ECOLI (P0A7E9)
Key		From		To		Description		Condition		FTGroup
NP_BIND		15		18		ATP (By similarity)		K-x-[SG]-G
NP_BIND		138		145		UMP (By similarity)
REGION (Optional)		23		28		Involved in allosteric activation by GTP (Potential)		G-x-x-G-x-G
BINDING		57		57		UMP; via amide nitrogen (By similarity)		G
BINDING		58		58		ATP; via amide nitrogen (By similarity)		G
BINDING		62		62		ATP (By similarity)		R
BINDING		77		77		UMP (By similarity)		D
BINDING (Optional)		165		165		ATP (By similarity)		T
BINDING (Optional)		166		166		ATP (By similarity)		[NQ]
BINDING		171		171		ATP; via amide nitrogen and carbonyl oxygen (By similarity)		[YF]
BINDING		174		174		ATP (By similarity)		[DE]

From: PYRH_SULSO (Q97ZE2)
Key		From		To		Description		Condition		FTGroup
NP_BIND (Optional)		7		11		ATP (By similarity)		K-x-[ST]-G-[KRS]
NP_BIND		114		120		UMP (By similarity)
BINDING		44		44		UMP; via amide nitrogen (By similarity)		G
BINDING		66		66		UMP (By similarity)		D
BINDING		45		45		ATP; via amide nitrogen (By similarity)		G
BINDING		49		49		ATP (By similarity)		R
BINDING (Optional)		140		140		ATP (By similarity)		[TS]
BINDING (Optional)		141		141		ATP (By similarity)		N
BINDING		146		146		ATP; via amide nitrogen and carbonyl oxygen (By similarity)		[YF]
BINDING		149		149		ATP (By similarity)		[DE]

From: PYRH_PYRFU (Q8U122)
Key		From		To		Description		Condition		FTGroup
NP_BIND		9		10		ATP (By similarity)		G-S

Size range:

231-266 amino acids

Size range:

217-241 amino acids

Related UniRules:	None
Template:	P0A7E9 (PYRH_ECOLI); O31749 (PYRH_BACSU); Q9PPX6 (PYRH_UREPA); Q8U122 (PYRH_PYRFU); Q97ZE2 (PYRH_SULSO); Q97R83 (PYRH_STRPN); P65933 (PYRH_SALTY); P43890 (PYRH_HAEIN); P65932 (PYRH_NEIMB); Q831V1 (PYRH_ENTFA); Q2FZ22 (PYRH_STAA8); P65938 (PYRH_STRP1); O28237 (PYRH_ARCFU); Q9Z5K8 (PYRH_LACLM): [Recover all]
Scope:	Bacteria Archaea
Fusion:	Nter: None; Cter: None
Duplicate:	None
Plasmid encoded:	None
Comments:	Archaea (SULSO) and UREPA are shown not to be allosterically activated by GTP. This may be due to the absence of a little region containing the motif GXXGXG in the N-terminal part of the enzyme, which could be involved in activation by GTP (see PubMed:18021254). Thus, the activation is automatically annotated via the presence/absence of this region, but the motif GXXGXG is maybe too strict, since NEIMB, that possesses the motif GSDPFG is also shown to be activated by GTP. Two magnesium ions are seen in the catalytic site of PYRFU, but only one in that of SULSO, which binds the phosphate groups of both ATP and UMP. Magnesium 1 annotated in PYRFU could have a catalytic role in the phosphoryl group transfer, a role that could be taken in charge by a positively charged lysine residue in bacteria (Lys-15 in ECOLI) and some other archaea (included SULSO) (see PubMed:17297917). Since the exact catalytic mechanism is not very clear yet and the residues that bind magnesium are not well conserved, this is not annotated and propagated by the rule. Possible wrong start in DEIRA and SYNY3. Longer C-terminus in MYCPE; sequence not taken into account in size range.