Q9X112 (METE_THEMA) 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:	TM_1286

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	734 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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	3D-structure Complete proteome Reference 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 – 734

734

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172

PRO_0000098674

Sites

Metal binding

618

1

Zinc By similarity

Metal binding

620

1

Zinc By similarity

Metal binding

704

1

Zinc By similarity

Secondary structure

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734

Helix Strand Turn

Details...

Helix

16 – 25

10

Helix

31 – 52

22

Beta strand

57 – 59

3

Helix

66 – 73

8

Helix

79 – 81

3

Helix

87 – 94

8

Beta strand

101 – 104

4

Beta strand

111 – 114

4

Helix

128 – 137

10

Turn

138 – 140

3

Beta strand

144 – 148

5

Helix

150 – 155

6

Helix

167 – 190

24

Beta strand

196 – 199

4

Helix

201 – 204

4

Helix

209 – 220

12

Turn

221 – 224

4

Beta strand

227 – 230

4

Helix

239 – 243

5

Beta strand

248 – 253

6

Helix

259 – 267

9

Beta strand

273 – 280

8

Helix

290 – 300

11

Beta strand

303 – 309

7

Helix

311 – 313

3

Beta strand

323 – 325

3

Turn

326 – 328

3

Helix

329 – 331

3

Helix

335 – 349

15

Turn

362 – 365

4

Helix

368 – 375

8

Helix

379 – 381

3

Helix

388 – 399

12

Helix

416 – 426

11

Helix

432 – 453

22

Beta strand

456 – 458

3

Helix

468 – 473

6

Beta strand

476 – 480

5

Beta strand

487 – 490

4

Beta strand

493 – 495

3

Beta strand

499 – 505

7

Helix

512 – 520

9

Beta strand

526 – 531

6

Helix

533 – 538

6

Beta strand

540 – 542

3

Beta strand

544 – 546

3

Helix

548 – 568

21

Beta strand

573 – 577

5

Helix

580 – 583

4

Helix

589 – 591

3

Helix

592 – 606

15

Beta strand

613 – 618

6

Turn

625 – 627

3

Helix

628 – 631

4

Beta strand

637 – 642

6

Turn

644 – 648

5

Helix

649 – 651

3

Helix

652 – 655

4

Beta strand

662 – 667

6

Helix

679 – 689

11

Turn

690 – 692

3

Helix

695 – 697

3

Beta strand

698 – 701

4

Helix

711 – 731

21

Sequences

	Sequence		Length	Mass (Da)
	Q9X112 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 34B19187480D443B	FASTA	734	85,571
	10 20 30 40 50 60 MKAYAFGFPK IGEKREFKKA LEDFWKGKIT EEQFEEEMNK LRMYMVENYR KNVDVIPSNE 70 80 90 100 110 120 LSYYDFVLDT AVMVGAVPER FGEYRGLSTY FDMARGGKAL EMTKFFNTNY HYLVPEIETE 130 140 150 160 170 180 EFYLLENKPL EDYLFFKSKG IETAPWVIGP FTFLYLSKRN GEWIRRPNQM EKLLESLVSV 190 200 210 220 230 240 YKEVFEKLVE NGCKEILVNE PAFVCDLEKA HWDLILNVYR ELSEFPLTVF TYYDSVSDYE 250 260 270 280 290 300 ACVSLPVKRL HFDFVSNEEN LKNLEKHGFP EDKKLVAGVI NGRQPWKVDL RKVASLVEKL 310 320 330 340 350 360 GASAISNSCP LFHLPVTLEL ENNLPGGLKE KLAFAKEKLE ELKMLKDFLE GKTFDLPNVS 370 380 390 400 410 420 FEDFAVDLQA VERVRNLPED SFRREKEYTE RDRIQRERLN LPLFPTTTIG SFPQTPEVRK 430 440 450 460 470 480 MRSKYRKGEI SKEEYEAFIK EQIKKAIELQ EEIGLDVLVH GEFERTDMVE FFAEKLNGIA 490 500 510 520 530 540 TTQNGWVLSY GSRCYRPPII YGTVTRPEPM TLKEITYAQS LTEKPVKGML TGPVTIMSWS 550 560 570 580 590 600 YYREDIPERE IAYQIALAIN EEVKDLEEAG IKIVQIDEPA FREKAPIKKS KWPEYFEWAI 610 620 630 640 650 660 NAFNLAANAR PETQIHAHMC YSDFNEIIEY IHQLEFDVIS IEASRSKGEI ISAFENFKGW 670 680 690 700 710 720 IKQIGVGVWD IHSPAVPSIN EMREIVERVL RVLPKELIWI NPDCGLKTRN WDEVIPSLRN 730 MVALAKEMRE KFES

References

[1]

"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD36360.1.

PIR

E72271.

RefSeq

NP_229090.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T7L	X-ray	2.00	A/B	2-734	[»]
1XDJ	X-ray	2.20	A/B	2-734	[»]
1XPG	X-ray	2.59	A/B	2-732	[»]
1XR2	X-ray	2.35	A/B	2-734	[»]
3BQ5	X-ray	2.00	A/B	2-734	[»]
3BQ6	X-ray	2.10	A/B	2-734	[»]

ProteinModelPortal

Q9X112.

SMR

Q9X112. Positions 2-733.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

898197.

GenomeReviews

Gene locus TM_1286 in contig AE000512_GR.

KEGG

tma:TM1286.

NMPDR

fig|243274.1.peg.1274.

PATRIC

23937512. VBITheMar51294_1302.

TIGR

TM_1286.

Phylogenomic databases

HOGENOM

HBG287495.

OMA

RNIWRAN.

PhylomeDB

Q9X112.

ProtClustDB

PRK05222.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1286-MONOMER.

BRENDA

2.1.1.14. 6331.

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_THEMA

Accession

Primary (citable) accession number: Q9X112

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program