Q5HTR3 (METE_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	CJE1335

Organism

Campylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]

Taxonomic identifier

195099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 754	754	5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172		PRO_1000017236
Sites
	Metal binding	641	1	Zinc By similarity
	Metal binding	643	1	Zinc By similarity
	Metal binding	726	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HTR3 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 6851B61E9E82A42A	FASTA	754	86,980
	10 20 30 40 50 60 MKNSIISYPR IGANRELKFA IEKYFKNQSS KEELLKSAKD LRIRHWQEIQ KAGIDFIPSN 70 80 90 100 110 120 DFSLYDNVLD AAVLFNIVHT KYKNLNLDAL DEYFAQSRGY QGENGDVTAL AMKKWFNTNY 130 140 150 160 170 180 HYLVPECDNA DIIALTGDKI FKEYLEAKEL GIESKPVLIG IFTLFKLIAF KDEKTQKLAK 190 200 210 220 230 240 EKLLNAYIEL FDKLNELKVT WLELDEPYLV YDLSKEDIAL FEEFYQELLN HKKDLKILLQ 250 260 270 280 290 300 SYFGDLRDIY PKLLESKFDA LGLDFIEGKQ SLALVQKYGF AKDKILFAGL INGKNIYTND 310 320 330 340 350 360 YAKSLKLIKE LQKYTQNIIL NTSCSLLHVP YSTEFESKLD SNYLKLFSFA KEKLQELKDL 370 380 390 400 410 420 KEILNSSEEN PLFRANQELF KNIPERLDEK VKARLKALKK EDFTRTPSFK ERALIQKEFL 430 440 450 460 470 480 KLPLLPTTTI GSFPQSADVR SNRLAFKQEK ISAQNYTEFN QQKIKECIQI QEEIGLDVLV 490 500 510 520 530 540 HGEFERNDMV EYFGENLKGF LFTQNGWVQS YGTRCVKPPV IWGDVSRTKP ITLAWSKFAQ 550 560 570 580 590 600 SLSQKIVKGM LTGPVTILNW SFPREDISLK ESTEQIALAI RDEVLDLENA GIKIIQIDEA 610 620 630 640 650 660 ALREKLPLRK SDWHSEYLDW AIPAFNLVHS GVKAKTQIHT HMCYSEFSDI LKEIDAMDAD 670 680 690 700 710 720 VISFEASRSN LSLLDTLKAI RFKTEVGPGV YDIHSPRVPS VEELSLTIEK ILNKLPKEQI 730 740 750 WINPDCGLKT RAYEEVIASL KNLVTATQKI REQL

References

[1]

"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species." Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. , Badger J.H., Fraser C.M., Nelson K.E. PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RM1221.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000025 Genomic DNA. Translation: AAW35656.1.
RefSeq	YP_179322.1. NC_003912.7.
3D structure databases
HSSP	HSSP built from PDB template 1U1J based on UniProtKB O50008.
ProteinModelPortal	Q5HTR3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HTR3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3231842.
GenomeReviews	Gene locus CJE1335 in contig CP000025_GR.
KEGG	cjr:CJE1335.
NMPDR	fig|195099.3.peg.1374.
PATRIC	20044470. VBICamJej134361_1353.
TIGR	CJE1335.
Phylogenomic databases
eggNOG	COG0620.
HOGENOM	HBG287495.
OMA	RNIWRAN.
ProtClustDB	PRK05222.
Enzyme and pathway databases
BioCyc	CJEJ195099:CJE_1335-MONOMER.
Family and domain databases
HAMAP	MF_00172. Meth_synth. [Tree]
InterPro	IPR013215. Cbl-indep_Met_Synth_N. IPR006276. Cobalamin-indep_Met_synthase. IPR002629. Methionine_synth. [Graphical view]
KO	K00549.
Pfam	PF08267. Meth_synt_1. 1 hit. PF01717. Meth_synt_2. 1 hit. [Graphical view]
PIRSF	PIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMs	TIGR01371. Met_syn_B12ind. 1 hit.
ProtoNet	Search...

Entry information

Entry name

METE_CAMJR

Accession

Primary (citable) accession number: Q5HTR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program