A9NF20 (METK_ACHLI) 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:	ACL_0328

Organism

Acholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]

Taxonomic identifier

441768 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	386 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 MF_00086
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP MF_00086
Cofactor	Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity. Binds 1 potassium ion per subunit By similarity. HAMAP MF_00086
Pathway	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. HAMAP MF_00086
Subunit structure	Homotetramer By similarity. HAMAP MF_00086
Subcellular location	Cytoplasm By similarity HAMAP MF_00086.
Sequence similarities	Belongs to the AdoMet synthase family.

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
Gene Ontology (GO)
Biological process	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 386	386	S-adenosylmethionine synthase HAMAP MF_00086		PRO_1000075365
Regions
	Nucleotide binding	263 – 270	8	ATP Potential
Sites
	Metal binding	16	1	Magnesium By similarity
	Metal binding	42	1	Potassium By similarity
	Metal binding	267	1	Potassium By similarity
	Metal binding	275	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9NF20 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 58DC321959A82ACA	FASTA	386	42,288
	10 20 30 40 50 60 MSYIFSSESV SKGHPDKVAD FIADSVLDLV LKNDPKARCA IEVALAHTTV YIFGEVSTSY 70 80 90 100 110 120 ILTDEIIIET AKKAIDFCGY NDEKFIFDAK SATYHVNIHK QSADIALGVD ETDNKEQGAG 130 140 150 160 170 180 DQGIMFGYAK DDTKELLPLP IFLAHELTKR LAFVREEGIV SGLGPDGKSQ VSVLYNENHE 190 200 210 220 230 240 PLEVTAIVLS TQHEASKTLE SVKADMMKHV ILEVIPKHLI TDNTKYYINP TGRFVIGGPV 250 260 270 280 290 300 GDSGLTGRKL IVDTYGGYSR HGGGAFSGKD ASKVDRSASY MARYLAKQVV GSGIAKTCEI 310 320 330 340 350 360 QLAYAIGVAE PVSLYVNTFG TSKVSNEVIA ETISKHFDLR PKAIINYLGL TNPIFKQTTH 370 380 NGHFGKLESN LSWEKLDKIE IFEQLV

References

[1]

"Complete genome and proteome of Acholeplasma laidlawii." Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I. , Alexeev D.G., Ladygina V.G., Govorun V.M. J. Bacteriol. 193:4943-4953(2011) [PubMed: 21784942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PG-8A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000896 Genomic DNA. Translation: ABX80950.1.
RefSeq	YP_001620326.1. NC_010163.1.
3D structure databases
ProteinModelPortal	A9NF20.
SMR	A9NF20. Positions 2-385.
ModBase	Search...
Protein-protein interaction databases
STRING	A9NF20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5804302.
GenomeReviews	Gene locus ACL_0328 in contig CP000896_GR.
KEGG	acl:ACL_0328.
PATRIC	20637376. VBIAchLai134690_0312.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG443662.
OMA	TQHAPGY.
Enzyme and pathway databases
BioCyc	ALAI441768:ACL_0328-MONOMER.
Family and domain databases
HAMAP	MF_00086. S-AdoMet_synth1. [Tree]
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]
KO	K00789.
PANTHER	PTHR11964. S-AdoMet_synt. 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_ACHLI

Accession

Primary (citable) accession number: A9NF20

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program