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Protein

Carboxy-S-adenosyl-L-methionine synthase

Gene

cmoA

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).UniRule annotation

Catalytic activityi

Prephenate + S-adenosyl-L-methionine = phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei38S-adenosyl-L-methionineUniRule annotation1 Publication1
Binding sitei131S-adenosyl-L-methionineUniRule annotation1 Publication1
Binding sitei198S-adenosyl-L-methionineUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxy-S-adenosyl-L-methionine synthaseUniRule annotation (EC:2.1.3.-UniRule annotation)
Short name:
Cx-SAM synthaseUniRule annotation
Gene namesi
Name:cmoAUniRule annotation
Ordered Locus Names:HI_0319
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001690841 – 241Carboxy-S-adenosyl-L-methionine synthaseAdd BLAST241

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi71421.HI0319.

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 34Combined sources14
Helixi38 – 52Combined sources15
Beta strandi58 – 63Combined sources6
Helixi68 – 75Combined sources8
Beta strandi83 – 87Combined sources5
Helixi91 – 102Combined sources12
Beta strandi110 – 113Combined sources4
Turni117 – 119Combined sources3
Beta strandi124 – 132Combined sources9
Helixi134 – 136Combined sources3
Helixi139 – 141Combined sources3
Helixi142 – 152Combined sources11
Beta strandi153 – 164Combined sources12
Helixi170 – 186Combined sources17
Helixi189 – 191Combined sources3
Helixi195 – 204Combined sources10
Helixi210 – 220Combined sources11
Beta strandi223 – 231Combined sources9
Beta strandi234 – 240Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IM8X-ray2.20A/B1-241[»]
ProteinModelPortaliP43985.
SMRiP43985.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43985.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 65S-adenosyl-L-methionine bindingUniRule annotation1 Publication3
Regioni88 – 89S-adenosyl-L-methionine bindingUniRule annotation1 Publication2
Regioni116 – 117S-adenosyl-L-methionine bindingUniRule annotation1 Publication2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DA6. Bacteria.
COG0500. LUCA.
KOiK15256.
OMAiMIELYYL.
PhylomeDBiP43985.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01589. Cx_SAM_synthase. 1 hit.
InterProiIPR005271. CmoA.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF006325. MeTrfase_bac. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00740. TIGR00740. 1 hit.

Sequencei

Sequence statusi: Complete.

P43985-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKDTLFSTP IAKLGDFIFD ENVAEVFPDM IQRSVPGYSN IITAIGMLAE
60 70 80 90 100
RFVTADSNVY DLGCSRGAAT LSARRNINQP NVKIIGIDNS QPMVERCRQH
110 120 130 140 150
IAAYHSEIPV EILCNDIRHV EIKNASMVIL NFTLQFLPPE DRIALLTKIY
160 170 180 190 200
EGLNPNGVLV LSEKFRFEDT KINHLLIDLH HQFKRANGYS ELEVSQKRTA
210 220 230 240
LENVMRTDSI ETHKVRLKNV GFSQVELWFQ CFNFGSMIAV K
Length:241
Mass (Da):27,372
Last modified:November 1, 1995 - v1
Checksum:i08743633A3E853F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC21983.1.
PIRiC64006.
RefSeqiNP_438485.1. NC_000907.1.
WP_005694346.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC21983; AAC21983; HI_0319.
GeneIDi949432.
KEGGihin:HI0319.
PATRICi20189181. VBIHaeInf48452_0337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC21983.1.
PIRiC64006.
RefSeqiNP_438485.1. NC_000907.1.
WP_005694346.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IM8X-ray2.20A/B1-241[»]
ProteinModelPortaliP43985.
SMRiP43985.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0319.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC21983; AAC21983; HI_0319.
GeneIDi949432.
KEGGihin:HI0319.
PATRICi20189181. VBIHaeInf48452_0337.

Phylogenomic databases

eggNOGiENOG4105DA6. Bacteria.
COG0500. LUCA.
KOiK15256.
OMAiMIELYYL.
PhylomeDBiP43985.

Miscellaneous databases

EvolutionaryTraceiP43985.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01589. Cx_SAM_synthase. 1 hit.
InterProiIPR005271. CmoA.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF006325. MeTrfase_bac. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00740. TIGR00740. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCMOA_HAEIN
AccessioniPrimary (citable) accession number: P43985
Secondary accession number(s): P43986
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 123 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.