B0CG96 (METK_ACAM1) 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:	AM1_5701

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length	418 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 – 418	418	S-adenosylmethionine synthase HAMAP MF_00086		PRO_1000075364
Regions
	Nucleotide binding	280 – 287	8	ATP Potential
Sites
	Metal binding	18	1	Magnesium By similarity
	Metal binding	44	1	Potassium By similarity
	Metal binding	284	1	Potassium By similarity
	Metal binding	292	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0CG96 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: DCE4ACC6D28D671B	FASTA	418	44,887
	10 20 30 40 50 60 MPKRYLFTSE SVTEGHPDKV CDQISDTILD ALLSQDPASR VAAEVVVNTG LVLLTGEITT 70 80 90 100 110 120 KAQVNFVDLV RQKITEIGYT DSDNGFAANS CSVLVALDEQ SPDIAQGVDS AQETREEKSD 130 140 150 160 170 180 QELDAIGAGD QGLMFGFACN ETPELMPLPI SLAHRVTRRL AAVRKTQLGY LRPDGKSQVT 190 200 210 220 230 240 VTYEDGRPVG IDTILVSTQH DATIGDITDP AAVQAKIKED LWNAVVLPVF ADIDIKPDDN 250 260 270 280 290 300 TRFLVNPTGQ FVVGGPQGDA GLTGRKIIVD TYGGYSRHGG GAFSGKDPTK VDRSAAYACR 310 320 330 340 350 360 YVAKNIVAAG LAEKCEVQLS YAIGVARPVS ILIETFGTGK VDEDRLLQVV QENFELRPAG 370 380 390 400 410 LIQTFGLTKL PGERGGRFYQ DVAAYGHFGR TDLDLPWEAT DKADLLKQAL SPALSGNA

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MBIC 11017.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000828 Genomic DNA. Translation: ABW30649.1.
RefSeq	YP_001519968.1. NC_009925.1.
3D structure databases
ProteinModelPortal	B0CG96.
SMR	B0CG96. Positions 3-411.
ModBase	Search...
Protein-protein interaction databases
STRING	B0CG96.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5684490.
GenomeReviews	Gene locus AM1_5701 in contig CP000828_GR.
KEGG	amr:AM1_5701.
PATRIC	20625384. VBIAcaMar40141_5297.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG443662.
OMA	IYYAHRL.
PhylomeDB	B0CG96.
ProtClustDB	PRK05250.
Enzyme and pathway databases
BioCyc	AMAR329726:AM1_5701-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_ACAM1

Accession

Primary (citable) accession number: B0CG96

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program