Q2RMS5 (METK2_RHORT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase 2
Short name=AdoMet synthase 2
EC=2.5.1.6

Alternative name(s):
MAT 2
Methionine adenosyltransferase 2

Gene names

Name:	metK2
Ordered Locus Names:	Rru_A3776

Organism

Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255)

Taxonomic identifier

269796 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length	389 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 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 Reference 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 – 389	389	S-adenosylmethionine synthase 2 HAMAP MF_00086		PRO_0000241031
Regions
	Nucleotide binding	261 – 268	8	ATP Potential
Sites
	Metal binding	19	1	Magnesium By similarity
	Metal binding	45	1	Potassium By similarity
	Metal binding	265	1	Potassium By similarity
	Metal binding	273	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2RMS5 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: ACA92D1AB22BC240	FASTA	389	41,753
	10 20 30 40 50 60 MAQSEYLFTS ESVSEGHPDK VCDRISDAIV DAFLAEDPHS RVALETMATT NFVVLAGEVR 70 80 90 100 110 120 GPDSLTHDRL KEIAREAIKD IGYEQRGFHW KDAEIVSHVH SQSADIAVGV DAAGNKDEGA 130 140 150 160 170 180 GDQGIMFGYA CTETEELMPA PIALSHAILK SLAEFRHGGD TSFGPDSKSQ VTLRYVDGKP 190 200 210 220 230 240 VGAASVVVST QHAGNLSQDE VRELVRPHVL KVLPEGWMCP EEEFYVNPTG RFVIGGPDGD 250 260 270 280 290 300 CGLTGRKIIV DTYGGAAPHG GGAFSGKDPT KVDRSAAYAA RYLAKNVVAA GLAEKCVIQV 310 320 330 340 350 360 SYAIGVSKPL SVYVNTQGTG QVDEQRLAVV LQQLMDLSPR GIRQHLQLSR PIYARTAAYG 370 380 HFGRKPEKDG GFSWERTDLV AGLKTAFGA

References

[1]

"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C. Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11170 / NCIB 8255.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000230 Genomic DNA. Translation: ABC24570.1.
RefSeq	YP_428857.1. NC_007643.1.
3D structure databases
ProteinModelPortal	Q2RMS5.
SMR	Q2RMS5. Positions 4-388.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2RMS5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3837233.
GenomeReviews	Gene locus Rru_A3776 in contig CP000230_GR.
KEGG	rru:Rru_A3776.
NMPDR	fig|1085.1.peg.1139.
PATRIC	23331364. VBIRhoRub82919_3898.
Phylogenomic databases
eggNOG	COG0192.
HOGENOM	HBG443662.
OMA	QDGFHWK.
PhylomeDB	Q2RMS5.
ProtClustDB	PRK05250.
Enzyme and pathway databases
BioCyc	RRUB269796:RRU_A3776-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

METK2_RHORT

Accession

Primary (citable) accession number: Q2RMS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program