P56878 (METK_RICPR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase
Short name=AdoMet synthase
EC=2.5.1.6

Alternative name(s):
MAT
Methionine adenosyltransferase

Gene names

Name:	metK
Ordered Locus Names:	RP777

Organism

Rickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]

Taxonomic identifier

272947 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › Rickettsia prowazekii

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme By similarity. HAMAP-Rule MF_00086
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP-Rule MF_00086
Cofactor	Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity. Binds 1 potassium ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. HAMAP-Rule MF_00086
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the AdoMet synthase family.
Caution	Non-functional in strain Madrid E.
Sequence caution	The sequence AJ235273 differs from that shown. Reason: Erroneous termination at position 141. Translated as Tyr.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP methionine adenosyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 380	380	S-adenosylmethionine synthase HAMAP-Rule MF_00086		PRO_0000174578
Regions
	Nucleotide binding	260 – 267	8	ATP Potential
Sites
	Metal binding	17	1	Magnesium By similarity
	Metal binding	43	1	Potassium By similarity
	Metal binding	264	1	Potassium By similarity
	Metal binding	272	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56878 [UniParc]. Last modified May 30, 2000. Version 1. Checksum: D1B29BB64481FBCA	FASTA	380	42,149
	10 20 30 40 50 60 MKNFVFTSES VSEGHPDKIA DQISDAVLDE ILKHDPNGRV ACETFVTTGL VLVGGEITTN 70 80 90 100 110 120 TYVDIEQVVR NKIQEIGYNN PNYGFDGSCC AVISSIIKQS PDIAMGIDNE NEEEIGAGDQ 130 140 150 160 170 180 GMVFGYACNE TKSLMPAPIY YAHLLMKRQA YLRKQNILSW LRPDAKSQVT LRYENNKPIV 190 200 210 220 230 240 IDSVVLSTQH HPEIQQKDLI EAVIEEIIKP TLPTNLLHKD TKYLINPTGR FVIGGPVADC 250 260 270 280 290 300 GLTGRKIIVD SYGGMAKHGG GCFSGKDPTK IDRSAAYMAR YIAKNIVGAG LADRCEIQIS 310 320 330 340 350 360 YAIGVADPVS VYAETFGTSK LSNEQTTKLI TEHFDMRPGK IIKNLKLHTQ CYQKTATYGH 370 380 FGREDENFTW EQLDKVDIFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E.
[2]	"Genome degradation is an ongoing process in Rickettsia." Andersson J.O., Andersson S.G.E. Mol. Biol. Evol. 16:1178-1191(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ235273 Genomic DNA. No translation available. AJ238756 Genomic DNA. Translation: CAB56090.1.
3D structure databases
ProteinModelPortal	P56878.
SMR	P56878. Positions 5-380.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00315; UER00080.
Family and domain databases
HAMAP	MF_00086. S-AdoMet_synth1.
InterPro	IPR022631. ADOMET_SYNTHASE_CS. IPR022630. S-AdoMet_synt_C. IPR022629. S-AdoMet_synt_central. IPR022628. S-AdoMet_synt_N. IPR002133. S-AdoMet_synthetase. IPR022636. S-AdoMet_synthetase_sfam. [Graphical view]
PANTHER	PTHR11964. PTHR11964. 1 hit.
Pfam	PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit. [Graphical view]
PIRSF	PIRSF000497. MAT. 1 hit.
SUPFAM	SSF55973. S-AdoMet_synt. 3 hits.
TIGRFAMs	TIGR01034. metK. 1 hit.
PROSITE	PS00376. ADOMET_SYNTHASE_1. 1 hit. PS00377. ADOMET_SYNTHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK_RICPR

Accession

Primary (citable) accession number: P56878

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program