DB code: S00307

CATH domain	Related DB codes (homologues)
3.40.50.300 : Rossmann fold	S00527 S00547 S00548 S00550 S00554 S00555 S00671 S00672 S00676 S00680 S00682 S00913 S00914 S00301 S00302 S00303 S00304 S00308 S00305 S00306 S00309 S00310 S00311 M00114 M00199 D00129 D00130 D00540 M00186

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	RefSeq	Pfam
P08760	GTP:AMP phosphotransferase mitochondrial	EC 2.7.4.10 Adenylate kinase 3 AK 3 Adenylate kinase 3 alpha-like 1	NP_776662.1 (Protein) NM_174237.2 (DNA/RNA sequence)	PF00406 (ADK) PF05191 (ADK_lid) [Graphical View]

KEGG enzyme name
nucleoside-triphosphate---adenylate kinase guanosine triphosphate-adenylate kinase nucleoside triphosphate-adenosine monophosphate transphosphorylase GTP:AMP phosphotransferase isozyme 3 of adenylate kinase

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
P08760	KAD3_BOVIN	NTP + AMP = NDP + ADP.	Monomer.	Mitochondrion matrix.

KEGG Pathways
Map code	Pathways	E.C.
MAP00240	Pyrimidine metabolism

Compound table
	Substrates		Products		Intermediates
KEGG-id	C00044	C00020	C00035	C00008
E.C.
Compound	GTP	AMP	GDP	ADP
Type	amide group,amine group,nucleotide	amine group,nucleotide	amide group,amine group,nucleotide	amine group,nucleotide
ChEBI	15996 15996	16027 16027	17552 17552	16761 16761
PubChem	6830 6830	6083 6083	8977 8977	6022 6022

1ak3A	Unbound	Bound:AMP	Unbound	Unbound
1ak3B	Unbound	Bound:AMP	Unbound	Unbound
2ak3A	Unbound	Bound:AMP	Unbound	Unbound
2ak3B	Unbound	Bound:AMP	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
similar to S00305

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1ak3A	LYS 18;ARG 122
1ak3B	LYS 18;ARG 122
2ak3A	LYS 18;ARG 122
2ak3B	LYS 18;ARG 122

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID	3013690
Journal	FEBS Lett
Year	1986
Volume	202
Pages	303-8
Authors	Tomasselli AG, Frank R, Schiltz E
Title	The complete primary structure of GTP:AMP phosphotransferase from beef heart mitochondria.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID	2175649
Journal	Biochemistry
Year	1990
Volume	29
Pages	8138-44
Authors	Diederichs K, Schulz GE
Title	Three-dimensional structure of the complex between the mitochondrial matrix adenylate kinase and its substrate AMP.
Related PDB	1ak3
Related UniProtKB	P08760
[3]
Resource
Comments
Medline ID
PubMed ID	1994037
Journal	J Mol Biol
Year	1991
Volume	217
Pages	541-9
Authors	Diederichs K, Schulz GE
Title	The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution.
Related PDB	2ak3
Related UniProtKB	P08760
[4]
Resource
Comments
Medline ID
PubMed ID	8537371
Journal	J Biol Chem
Year	1995
Volume	270
Pages	31103-10
Authors	Schricker R, Magdolen V, Strobel G, Bogengruber E, Breitenbach M, Bandlow W
Title	Strain-dependent occurrence of functional GTP:AMP phosphotransferase (AK3) in Saccharomyces cerevisiae.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID	9665856
Journal	J Mol Biol
Year	1998
Volume	280
Pages	551-8
Authors	Yamada M, Sugahara M, Hishitani Y, Nobumoto M, Nakazawa A
Title	Isolation and characterization of mutated mitochondrial GTP:AMP phosphotransferase.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the adenylate kinase family. This enzyme, adenylate kinase isozyme-3 (GTP:AMP phosphotransferase), is related to other adenylate kinases (see S00305).

Created	Updated
2002-05-31	2009-02-26