Reviewed, UniProtKB/Swiss-Prot P31153 (METK2_HUMAN)

Names and origin

Protein names

Recommended name:
    S-adenosylmethionine synthetase isoform type-2
      Short name=AdoMet synthetase 2
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 2
      Short name=MAT 2
    Methionine adenosyltransferase II
      Short name=MAT-II

Gene names

Name:	MAT2A
Synonyms:	AMS2, MATA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.
Cofactor	Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity. Binds 1 potassium ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subunit structure	Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B). Ref.7
Post-translational modification	The alpha' subunit is a post-translationally modified version of MAT2A.
Sequence similarities	Belongs to the AdoMet synthetase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Traceable author statement. Source: ProtInc potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 395

395

S-adenosylmethionine synthetase isoform type-2

PRO_0000174435

Regions

Nucleotide binding

131 – 136

6

ATP Potential

Sites

Metal binding

31

1

Magnesium By similarity

Metal binding

57

1

Potassium By similarity

Metal binding

283

1

Potassium By similarity

Metal binding

291

1

Magnesium By similarity

Binding site

159

1

ATP Potential

Amino acid modifications

Modified residue

81

1

N6-acetyllysine Ref.10

Modified residue

114

1

Phosphoserine Ref.8

Secondary structure

1

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395

Helix Strand Turn

Details...

Beta strand

17 – 25

9

Helix

30 – 48

19

Beta strand

53 – 61

9

Beta strand

64 – 72

9

Helix

79 – 90

12

Helix

95 – 97

3

Turn

101 – 103

3

Beta strand

104 – 111

8

Helix

115 – 121

7

Turn

122 – 124

3

Helix

127 – 129

3

Beta strand

132 – 134

3

Beta strand

136 – 143

8

Helix

152 – 169

18

Beta strand

176 – 191

16

Beta strand

194 – 209

16

Helix

215 – 224

10

Helix

227 – 230

4

Helix

233 – 235

3

Beta strand

241 – 245

5

Helix

254 – 256

3

Turn

266 – 273

8

Helix

290 – 307

18

Beta strand

312 – 320

9

Beta strand

328 – 333

6

Helix

342 – 352

11

Helix

357 – 364

8

Turn

365 – 367

3

Helix

371 – 374

4

Beta strand

375 – 377

3

Beta strand

379 – 382

4

Helix

386 – 388

3

Sequences

	Sequence		Length	Mass (Da)
	P31153-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 2E7D1B91CC4F7BDD	FASTA	395	43,661
	10 20 30 40 50 60 MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA 70 80 90 100 110 120 KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG 130 140 150 160 170 180 VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS 190 200 210 220 230 240 KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT 250 260 270 280 290 300 IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 310 320 330 340 350 360 VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI 370 380 390 VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase." Horikawa S., Tsukada K. FEBS Lett. 312:37-41(1992) [PubMed: 1426236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Activation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia." Panayiotidis M.I., Stabler S.P., Ahmad A., Pappa A., Legros L.H. Jr., Hernandez-Saavedra D., Schneider B.K., Allen R.H., Vasiliou V., McCord J.M., Kotb M., White C.W. Free Radic. Biol. Med. 40:348-358(2006) [PubMed: 16413417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[7]	"Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II)." LeGros H.L., Halim A.-B., Geller A.M., Kotb M. J. Biol. Chem. 275:2359-2366(2000) [PubMed: 10644686] [Abstract] Cited for: SUBUNIT.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X68836 mRNA. Translation: CAA48726.1.
DQ083239 mRNA. Translation: AAY85355.1.
AK291126 mRNA. Translation: BAF83815.1.
AC016753 Genomic DNA. Translation: AAY24339.1.
CH471053 Genomic DNA. Translation: EAW99511.1.
BC001686 mRNA. Translation: AAH01686.1.
BC001854 mRNA. Translation: AAH01854.1.

IPI

IPI00010157.

PIR

S27257.

RefSeq

NP_005902.1.

UniGene

Hs.516157

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P02	X-ray	1.21	A	1-395	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P31153. 6 interactions.

STRING

P31153.

PTM databases

PhosphoSite

P31153.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00010157.

Proteomic databases

PeptideAtlas

P31153.

PRIDE

P31153.

Genome annotation databases

Ensembl

ENST00000306434; ENSP00000303147; ENSG00000168906; Homo sapiens. [Genome view]
ENST00000409017; ENSP00000386353; ENSG00000168906; Homo sapiens. [Genome view]
ENST00000410008; ENSP00000386436; ENSG00000168906; Homo sapiens. [Genome view]
ENST00000417859; ENSP00000403128; ENSG00000168906; Homo sapiens. [Genome view]
ENST00000424323; ENSP00000399088; ENSG00000168906; Homo sapiens. [Genome view]
ENST00000450355; ENSP00000391050; ENSG00000168906; Homo sapiens. [Genome view]

GeneID

4144.

KEGG

hsa:4144.

NMPDR

fig|9606.3.peg.18145.

UCSC

uc002spr.1. human.

Organism-specific databases

CTD

4144.

GeneCards

GC02P085619.

H-InvDB

HIX0002218.

HGNC

HGNC:6904. MAT2A.

MIM

601468. gene.

PharmGKB

PA30647.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P31153.

HOVERGEN

P31153.

OMA

FHDAFIE.

Enzyme and pathway databases

BRENDA

2.5.1.6. 247.

Reactome

REACT_13. Metabolism of amino acids.
REACT_13433. Biological oxidations.

Gene expression databases

ArrayExpress

P31153.

Bgee

P31153.

CleanEx

HS_MAT2A.

Genevestigator

P31153.

GermOnline

ENSG00000168906. Homo sapiens.

Family and domain databases

InterPro

IPR002133. S-AdoMet_synthetase.
[Graphical view]

PANTHER

PTHR11964. S-AdoMet_synt. 1 hit.

Pfam

PF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000497. MAT. 1 hit.

TIGRFAMs

TIGR01034. metK. 1 hit.

PROSITE

PS00376. ADOMET_SYNTHETASE_1. 1 hit.
PS00377. ADOMET_SYNTHETASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

NextBio

16276.

SOURCE

Search...

Entry information

Entry name

METK2_HUMAN

Accession

Primary (citable) accession number: P31153
Secondary accession number(s): A8K511, Q53SP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	November 3, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.