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A5G0M4 (METE_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

EC=2.1.1.14
Alternative name(s):
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Gene names
Name:metE
Ordered Locus Names:Acry_2208
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation By similarity. HAMAP MF_00172

Catalytic activity

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. HAMAP MF_00172

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00172

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. HAMAP MF_00172

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7697695-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
PRO_1000017214

Sites

Metal binding6501Zinc By similarity
Metal binding6521Zinc By similarity
Metal binding7381Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A5G0M4 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: C0A580C41034C5B6

FASTA76984,014
        10         20         30         40         50         60 
MSIATSLGFP RIGRRRELKS ALEAHWAGEL SEAGLQEAAR LLRAESHSLQ QGLGIGHIPS 

        70         80         90        100        110        120 
NDFALYDHVL DTACMVGAIP PGYGWRGGEV TLPTYFALAR GTGGGDAAAG LPALEMTKWF 

       130        140        150        160        170        180 
DTNYHYLVPR LAAGQHFAVT ANRPLALFRE ALARHRRTRP VLLGPVSFLL LAKTDDGSDP 

       190        200        210        220        230        240 
LDLLDRLLPC YAQVLAELAA EGCAWVQMDE PVLALDLAPK ARAALRHAYE TLARGATPRL 

       250        260        270        280        290        300 
LLASYFAPIA DNLPTALALP VAGLHLDLVR GRDDLAPVLA AIGPATWLSL GLVDGRNVWR 

       310        320        330        340        350        360 
ADLRAALATA REAARALGGS ERLMIAPSCS LLHVPVDLAQ EDRLDPAIRP WLAFATQKLA 

       370        380        390        400        410        420 
EVATIARGLD EGEGAIAEAL EASDAALRTR RDSARVHRTD VAARLLGATP EMERRPAPHA 

       430        440        450        460        470        480 
ARRARQRQRL PLPAFPTTTI GSLPQTSGVR RTRAALARGE IGAAEYDEAI ATWTEDAIRL 

       490        500        510        520        530        540 
QERIGLDVLV HGEFERNDMV KYFGEQLDGF AFTRHGWVQS YGSRCVAPPI IWGDVARPRP 

       550        560        570        580        590        600 
MTVRWARHAQ SLTARPVKGM LTGPVTMLQW SFVRDDLPRE TVCRQIALAL RDEVADLEAA 

       610        620        630        640        650        660 
GLAIIQVDEP AFREGLPLRT ADREAYLRWA VSCFRLATAV VRDDTAIHTH MCYAEFQDIM 

       670        680        690        700        710        720 
PAIATMDADA ISIETARSRM ELLEAFAGHG PSAYPAEIGP GVWDIHSPRI PPEEEILALL 

       730        740        750        760 
RLARRKLADD QLWVNPDCGL KTRNWREVIP ALENLVGAAR RLRAEAIPA 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000697 Genomic DNA. Translation: ABQ31406.1.
RefSeqYP_001235325.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5G0M4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5G0M4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5159808.
GenomeReviewsGene locus Acry_2208 in contig CP000697_GR.
KEGGacr:Acry_2208.
PATRIC20649496. VBIAciCry6074_2718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0620.
HOGENOMHBG287495.
OMARNIWRAN.
ProtClustDBPRK05222.

Enzyme and pathway databases

BioCycACRY349163:ACRY_2208-MONOMER.

Family and domain databases

HAMAPMF_00172. Meth_synth.
[Tree]
InterProIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Methionine_synth.
[Graphical view]
KOK00549.
PfamPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsTIGR01371. Met_syn_B12ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMETE_ACICJ
AccessionPrimary (citable) accession number: A5G0M4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families