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Q83A78

- METK_COXBU

UniProt

Q83A78 - METK_COXBU

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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
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

Binds 2 divalent ions per subunit. Magnesium or cobalt.UniRule annotation
Binds 1 potassium ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181MagnesiumUniRule annotation
Metal bindingi44 – 441PotassiumUniRule annotation
Metal bindingi265 – 2651PotassiumUniRule annotation
Metal bindingi273 – 2731MagnesiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi261 – 2688ATPUniRule 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

BioCyciCBUR227377:GJ7S-2004-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:CBU_2030
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000002671: 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 – 393393S-adenosylmethionine synthasePRO_0000174514Add
BLAST

Proteomic databases

PRIDEiQ83A78.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi227377.CBU_2030.

Structurei

3D structure databases

ProteinModelPortaliQ83A78.
SMRiQ83A78. Positions 6-386.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0192.
HOGENOMiHOG000245710.
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.

Q83A78-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTHTTLFTSE SVSEGHPDKV ADQISDAVLD ALIGQDPNCR VACEAVVKSG
60 70 80 90 100
MVFVAGEITT NAWADVEQIT RNTVLQIGYN DPHLGFDGET CAVVTAIGKQ
110 120 130 140 150
SPDIVMGVDG REDQELGAGD QGLMFGYASR ETNVFMPAPI TYAHRLVRQQ
160 170 180 190 200
ALLRKNGRLP WLRPDAKSQV TLRYENGKPV AADCIVLSTQ HSPEISQESL
210 220 230 240 250
REAVIDEIIK PIMPPHWLDK HTRFLVNPTG RFVIGGPVGD CGLTGRKIIV
260 270 280 290 300
DTYGGMARHG GGCFSGKDPS KVDRSGAYAA RYVAKNIVAG GLADRCEIQV
310 320 330 340 350
SYAIGVAEPT SISVETFGTG KIDEVRIQQL IKEHFDLRPG KIIEELNLLR
360 370 380 390
SIYKATATYG HFGREEPEFT WERTDKAEIL REAAGLAAAN VTN
Length:393
Mass (Da):42,777
Last modified:June 1, 2003 - v1
Checksum:i9AFBE2DA6A03929D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016828 Genomic DNA. Translation: AAO91517.1.
RefSeqiNP_821003.1. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO91517; AAO91517; CBU_2030.
GeneIDi1209943.
KEGGicbu:CBU_2030.
PATRICi17932813. VBICoxBur82552_2023.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016828 Genomic DNA. Translation: AAO91517.1 .
RefSeqi NP_821003.1. NC_002971.3.

3D structure databases

ProteinModelPortali Q83A78.
SMRi Q83A78. Positions 6-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227377.CBU_2030.

Proteomic databases

PRIDEi Q83A78.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO91517 ; AAO91517 ; CBU_2030 .
GeneIDi 1209943.
KEGGi cbu:CBU_2030.
PATRICi 17932813. VBICoxBur82552_2023.

Phylogenomic databases

eggNOGi COG0192.
HOGENOMi HOG000245710.
KOi K00789.
OMAi GYVNSEM.
OrthoDBi EOG68WR6M.

Enzyme and pathway databases

UniPathwayi UPA00315 ; UER00080 .
BioCyci CBUR227377:GJ7S-2004-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: RSA 493 / Nine Mile phase I.

Entry informationi

Entry nameiMETK_COXBU
AccessioniPrimary (citable) accession number: Q83A78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 81 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, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): 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