A0PKM7 (A0PKM7_MYCUA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172
EC=2.1.1.14 HAMAP MF_00172

Alternative name(s):
Cobalamin-independent methionine synthase HAMAP MF_00172
Methionine synthase, vitamin-B12 independent isozyme HAMAP MF_00172

Gene names

Name:	metE HAMAP MF_00172 EMBL ABL02896.1
Ordered Locus Names:	MUL_0138

Organism

Mycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]

Taxonomic identifier

362242 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	791 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 SAAS SAAS013215
Catalytic activity	5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. HAMAP MF_00172 SAAS SAAS013215
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 SAAS SAAS013215
Sequence similarities	Belongs to the vitamin-B12 independent methionine synthase family. HAMAP MF_00172

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis HAMAP MF_00172 SAAS SAAS013215
Domain	Repeat HAMAP MF_00172
Ligand	Metal-binding HAMAP MF_00172 SAAS SAAS013215 Zinc HAMAP MF_00172 SAAS SAAS013215
Molecular function	Methyltransferase HAMAP MF_00172 SAAS SAAS013215 EMBL ABL02896.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: HAMAP 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
Sites
	Metal binding	678	1	Zinc By similarity HAMAP MF_00172
	Metal binding	680	1	Zinc By similarity HAMAP MF_00172
	Metal binding	763	1	Zinc By similarity HAMAP MF_00172

Sequences

	Sequence		Length	Mass (Da)
	A0PKM7 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: CAABE9FC5AF02518	FASTA	791	85,128
	10 20 30 40 50 60 MLVRSKHGAV GSVVRPRAVI TPSIEGRAVI QLVSQQPFFA TITGSPRIGP RRELKRATEG 70 80 90 100 110 120 YWAGRTNRAE LESVAATLRR DTWTDLAAAG LDSVPVNTFS YYDQMLDTAV LLGALPTRVA 130 140 150 160 170 180 GICDDLDRYF AAARGNAEVS PLEMTKWFDT NYHYLVPEIG PDTRFGLHPD KVLAELKEAQ 190 200 210 220 230 240 ELGIRARPVV IGPVTFLLLS KAVDGASAPI GRLEELMPIY SELLSLLADS GAQWVQLDEP 250 260 270 280 290 300 ALVTDICPDA PALAERMYTA LGSLANRPAI HVATYFGDPG AALGALARTP IEAIGVDLVA 310 320 330 340 350 360 GAHTAIASIV AAPELADKTL VAGIVDGRNI WRTDLQAALS RLATLLGSAA SIAVSTSCST 370 380 390 400 410 420 LHVPYSLEPE TDLDASLRSW LAFGAEKVAE VAVLARALRE GREAVAAEIA ASNEAVASRK 430 440 450 460 470 480 KDPRLHNGQV RARIHAILAS GVHRGDAATR RLSQEARLQL PPLPTTTIGS YPQTTAIRTA 490 500 510 520 530 540 RAALRADEID EAEYARRMEK EIADVIALQE ELGLDVLVHG EPERNDMVQY FAEQLDGFFA 550 560 570 580 590 600 TQNGWVQSYG SRCVRPPILY GDVARSHPMT VDWISYAQSL TAKPVKGMLT GPVTILAWSF 610 620 630 640 650 660 VRDDQALPDT ANQVALAIRD ETVDLQSAGI AVIQVDEPAL RELLPLRRSE QDVYLRWAVA 670 680 690 700 710 720 AFRLATSGVA DSTQIHTHLC YSEFGEVIGA IADLDADVTS IEAARSHMEV LDDLNAIGFA 730 740 750 760 770 780 NSVGPGVYDI HSPRVPSAEE MADSLRAALK AVPAGRLWAN PDCGLKTRNV DEVTASLQNM 790 VAAAQKVRTE A

References

[1]

"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer." Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T. Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000325 Genomic DNA. Translation: ABL02896.1.
RefSeq	YP_904367.1. NC_008611.1.
3D structure databases
ProteinModelPortal	A0PKM7.
ModBase	Search...
Protein-protein interaction databases
STRING	A0PKM7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000076336; EBMYCP00000074341; EBMYCG00000076331.
GeneID	4552861.
GenomeReviews	Gene locus MUL_0138 in contig CP000325_GR.
KEGG	mul:MUL_0138.
PATRIC	18166737. VBIMycUlc37413_0248.
Organism-specific databases
GenoList	MUL_0138.
CMR	Search...
Phylogenomic databases
eggNOG	COG0620.
GeneTree	EBGT00050000017657.
HOGENOM	HBG287495.
OMA	RNIWRAN.
PhylomeDB	A0PKM7.
ProtClustDB	PRK05222.
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

A0PKM7_MYCUA

Accession

Primary (citable) accession number: A0PKM7

Entry history

Integrated into UniProtKB/TrEMBL:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	December 14, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)