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Q8K9E5

- METK_BUCAP

UniProt

Q8K9E5 - METK_BUCAP

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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation, Co2+UniRule annotationNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.UniRule annotation
  • K(+)UniRule annotationNote: Binds 1 potassium ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171MagnesiumUniRule annotation
Metal bindingi43 – 431PotassiumUniRule annotation
Metal bindingi264 – 2641PotassiumUniRule annotation
Metal bindingi272 – 2721MagnesiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi260 – 2678ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. methionine adenosyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. one-carbon metabolic process Source: UniProtKB-HAMAP
  2. S-adenosylmethionine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-413-MONOMER.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthaseUniRule annotation (EC:2.5.1.6UniRule annotation)
Short name:
AdoMet synthaseUniRule annotation
Alternative name(s):
MATUniRule annotation
Methionine adenosyltransferaseUniRule annotation
Gene namesi
Name:metKUniRule annotation
Ordered Locus Names:BUsg_393
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379S-adenosylmethionine synthasePRO_0000174503Add
BLAST

Proteomic databases

PRIDEiQ8K9E5.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi198804.BUsg393.

Structurei

3D structure databases

ProteinModelPortaliQ8K9E5.
SMRiQ8K9E5. Positions 3-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0192.
KOiK00789.
OMAiGYVNSEM.
OrthoDBiEOG68WR6M.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. 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]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K9E5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEYLFTSES VSEGHPDKIA DQISDALLDE IIKQDLKARV ACETYVKTGM
60 70 80 90 100
VLIGGEITTT AWVDVEEITR NTINNIGYIN SETGFDANSC AVLSTIGKQS
110 120 130 140 150
PDITQGVDRC NPLEQGAGDQ GIIFGYATNE TEVLMPAPIT YAHLLVKKQS
160 170 180 190 200
ELRKKNILHW LRPDAKSQVT FKYKNGRIIG IDTVVFSTQH KESITQDVLK
210 220 230 240 250
EAVMEEIIKP VLPNKWLTKN TKFFINPTGR FVIGGPMGDC GLTGRKIIVD
260 270 280 290 300
TYGGMSRHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQLS
310 320 330 340 350
YAIGIAEPTS IMIETFRTGK ISNKSLINLV RNIFDLRPYG LIEMLDLLRP
360 370
IYLNTAVYGH FGREEFPWEK LDKVDELLQ
Length:379
Mass (Da):42,003
Last modified:October 1, 2002 - v1
Checksum:i8D5576799F7DAFE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67945.1.
RefSeqiNP_660734.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67945; AAM67945; BUsg_393.
GeneIDi1005765.
KEGGibas:BUsg393.
PATRICi21247606. VBIBucAph100086_0406.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67945.1 .
RefSeqi NP_660734.1. NC_004061.1.

3D structure databases

ProteinModelPortali Q8K9E5.
SMRi Q8K9E5. Positions 3-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198804.BUsg393.

Proteomic databases

PRIDEi Q8K9E5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM67945 ; AAM67945 ; BUsg_393 .
GeneIDi 1005765.
KEGGi bas:BUsg393.
PATRICi 21247606. VBIBucAph100086_0406.

Phylogenomic databases

eggNOGi COG0192.
KOi K00789.
OMAi GYVNSEM.
OrthoDBi EOG68WR6M.

Enzyme and pathway databases

UniPathwayi UPA00315 ; UER00080 .
BioCyci BAPH198804:GHMG-413-MONOMER.

Family and domain databases

HAMAPi MF_00086. S_AdoMet_synth1.
InterProi 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 ]
PANTHERi PTHR11964. PTHR11964. 1 hit.
Pfami PF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000497. MAT. 1 hit.
SUPFAMi SSF55973. SSF55973. 3 hits.
TIGRFAMsi TIGR01034. metK. 1 hit.
PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiMETK_BUCAP
AccessioniPrimary (citable) accession number: Q8K9E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3