P31153 (METK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase isoform type-2
Short name=AdoMet synthase 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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
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 synthase 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 Reference proteome
Gene Ontology (GO)
Biological_process	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome methylation Traceable author statement. Source: Reactome one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW sulfur amino acid metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Traceable author statement PubMed 7665609. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 395

395

S-adenosylmethionine synthase 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.9

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CH471053 Genomic DNA. Translation: EAW99513.1.
BC001686 mRNA. Translation: AAH01686.1.
BC001854 mRNA. Translation: AAH01854.1.

IPI

IPI00010157.

PIR

S27257.

RefSeq

NP_005902.1. NM_005911.5.

UniGene

Hs.516157.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P31153.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31153. 17 interactions.

STRING

9606.ENSP00000303147.

PTM databases

PhosphoSite

P31153.

Polymorphism databases

DMDM

400245.

2D gel databases

REPRODUCTION-2DPAGE

IPI00010157.

Proteomic databases

PaxDb

P31153.

PeptideAtlas

P31153.

PRIDE

P31153.

Protocols and materials databases

DNASU

4144.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000306434; ENSP00000303147; ENSG00000168906.

GeneID

4144.

KEGG

hsa:4144.

UCSC

uc002spr.3. human.

Organism-specific databases

CTD

4144.

GeneCards

GC02P085766.

H-InvDB

HIX0117562.

HGNC

HGNC:6904. MAT2A.

HPA

CAB009968.
HPA043028.

MIM

601468. gene.

neXtProt

NX_P31153.

PharmGKB

PA30647.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0192.

HOGENOM

HOG000245710.

HOVERGEN

HBG001562.

InParanoid

P31153.

KO

K00789.

OMA

YAKTSAY.

OrthoDB

EOG4QVCC3.

PhylomeDB

P31153.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00315; UER00080.

Gene expression databases

ArrayExpress

P31153.

Bgee

P31153.

CleanEx

HS_MAT2A.

Genevestigator

P31153.

GermOnline

ENSG00000168906. Homo sapiens.

Family and domain databases

InterPro

IPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]

PANTHER

PTHR11964. PTHR11964. 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.

SUPFAM

SSF55973. S-AdoMet_synt. 3 hits.

TIGRFAMs

TIGR01034. metK. 1 hit.

PROSITE

PS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MAT2A. human.

DrugBank

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

EvolutionaryTrace

P31153.

GenomeRNAi

4144.

NextBio

16276.

SOURCE

Search...

Entry information

Entry name

METK2_HUMAN

Accession

Primary (citable) accession number: P31153
Secondary accession number(s): A8K511, D6W5L1, Q53SP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.