Methionine synthase - Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Methionine synthase
EC=2.1.1.13

Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Methionine synthase, vitamin-B12 dependent
Short name=MS

Gene names

Name:	metH
Ordered Locus Names:	PA1843

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length	1234 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate By similarity.
Catalytic activity	5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.
Cofactor	Cobalamin By similarity. Binds 1 zinc ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Domain	Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin By similarity.
Miscellaneous	L-homocysteine is bound via the zinc atom By similarity.
Sequence similarities	Belongs to the vitamin-B12 dependent methionine synthase family. Contains 1 AdoMet activation domain. Contains 1 B12-binding domain. Contains 1 B12-binding N-terminal domain. Contains 1 Hcy-binding domain. Contains 1 pterin-binding domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Domain	Repeat
Ligand	Cobalamin Cobalt Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pteridine-containing compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: InterPro methionine synthase 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 – 1234

1234

Methionine synthase

PRO_0000287780

Regions

Domain

12 – 332

321

Hcy-binding

Domain

363 – 624

262

Pterin-binding

Domain

655 – 749

95

B12-binding N-terminal

Domain

752 – 888

137

B12-binding

Domain

904 – 1234

331

AdoMet activation

Region

840 – 841

2

Cobalamin-binding By similarity

Region

1197 – 1198

2

S-adenosyl-L-methionine binding By similarity

Sites

Metal binding

254

1

Zinc By similarity

Metal binding

317

1

Zinc By similarity

Metal binding

318

1

Zinc By similarity

Metal binding

765

1

Cobalt (cobalamin axial ligand) By similarity

Binding site

810

1

Cobalamin By similarity

Binding site

954

1

S-adenosyl-L-methionine By similarity

Binding site

1142

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

1146

1

Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9I2Q2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9877F8AC8BEF44ED
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FASTA

1,234

135,063

        10         20         30         40         50         60 
MSSPLTDRSA RLQALQHALR ERILILDGGM GTMIQSYKLE EADYRGERFA DWPSDVKGNN 

        70         80         90        100        110        120 
DLLLLSRPDV IQAIEKAYLD AGADILETNT FNATQVSQAD YGMQSLAYEL NVEGARLARQ 

       130        140        150        160        170        180 
VADAKTAETP DKPRFVAGVL GPTSRTCSIS PDVNNPGYRN VTFDELVENY VEATRGLIEG 

       190        200        210        220        230        240 
GADLILIETI FDTLNAKAAI FAVQGVFEEL GVELPIMISG TITDASGRTL SGQTTEAFWN 

       250        260        270        280        290        300 
SVRHARPISV GLNCALGAKE LRPYIEELST KADTHVSAHP NAGLPNAFGE YDESPAEMAV 

       310        320        330        340        350        360 
VVEEFAAAGF LNIVGGCCGT TPAHIEAIAK AVAKYPPRAI PEIPRACRLS GLEPFTIDRS 

       370        380        390        400        410        420 
SLFVNVGERT NITGSAKFAR LIREENYAEA LEVAQQQVEA GAQVIDINMD EGMLDSKAAM 

       430        440        450        460        470        480 
VTFLNLIASE PDISRVPIMI DSSKWEVIEA GLKCIQGKGI VNSISMKEGV EAFKHHARLC 

       490        500        510        520        530        540 
KRYGAAVVVM AFDEDGQADT QARKEEICKR SYDILVDEVG FPPEDIIFDA NIFAIATGIE 

       550        560        570        580        590        600 
EHNNYAVDFI NACAYIRDNL PYALSSGGVS NVSFSFRGNN PVREAIHSVF LYYAIRNGLT 

       610        620        630        640        650        660 
MGIVNAGQLE IYDEIPKALR DRVEDVVLNR TPEATEALLA IADDYKGGGA VKEAEDEEWR 

       670        680        690        700        710        720 
SYSVEKRLEH ALVKGITTWI VEDTEECRQQ CARPIEVIEG PLMSGMNVVG DLFGAGKMFL 

       730        740        750        760        770        780 
PQVVKSARVM KQAVAHLIPF IEAEKGDKPE AKGKILMATV KGDVHDIGKN IVGVVLGCNG 

       790        800        810        820        830        840 
YDVVDLGVMV PAEKILQTAI AEKCDIIGLS GLITPSLDEM VHVAKEMQRQ NFQLPLMIGG 

       850        860        870        880        890        900 
ATTSKAHTAV KIDPQYSNDA VVYVTDASRA VGVATSLLSK ELKADYVART RADYAVVRER 

       910        920        930        940        950        960 
TANRSARTER LSYEQAIANK PAFDWAGYQA PTPSFTGVRV LDEIDLAVLA EYIDWTPFFI 

       970        980        990       1000       1010       1020 
SWDLAGKYPR ILTDEVVGEA ATSLFNDAQA MLKKLIDEKL IKARAVFGFW PANQVEHDDL 

      1030       1040       1050       1060       1070       1080 
EVYGADGETL ATLHHLRQQT IKPDGKPNLS LADFVAPKES GVRDYIGGFI TTAGIGAEEV 

      1090       1100       1110       1120       1130       1140 
AKAYEAKGDD YNSIMVKALA DRLAEACAEW LHERVRKEYW GYARDEHLDN EALIKEQYVG 

      1150       1160       1170       1180       1190       1200 
IRPAPGYPAC PDHTEKGTLF ELLDPQGLSG VSLTEHYAMF PAAAVSGWYF AHPQAQYFAV 

      1210       1220       1230 
GKIDKDQVER YSQRKGQEAS VSERWLAPNL GYDD

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References

[1]

"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R.

Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004091 Genomic DNA. Translation: AAG05232.1.
PIR	E83415.
RefSeq	NP_250534.1. NC_002516.2.
3D structure databases
HSSP	HSSP built from PDB template 1BMT based on UniProtKB P13009.
ProteinModelPortal	Q9I2Q2.
SMR	Q9I2Q2. Positions 19-646, 658-1233.
ModBase	Search...
Protein-protein interaction databases
STRING	208964.PA1843.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	880631.
KEGG	pae:PA1843.
PATRIC	19838071. VBIPseAer58763_1916.
Organism-specific databases
PseudoCAP	PA1843.
Phylogenomic databases
eggNOG	COG1410.
HOGENOM	HOG000251409.
KO	K00548.
OMA	VRKEFWG.
ProtClustDB	PRK09490.
Enzyme and pathway databases
UniPathway	UPA00051; UER00081.
Family and domain databases
Gene3D	1.10.1240.10. 1 hit. 3.10.196.10. 1 hit. 3.20.20.20. 1 hit. 3.20.20.330. 1 hit. 3.40.50.280. 1 hit.
InterPro	IPR003759. Cbl-bd_cap. IPR006158. Cobalamin-bd. IPR011005. Dihydropteroate_synth-like. IPR011822. MetH. IPR000489. Pterin-binding. IPR003726. S_MeTrfase. IPR004223. VitB12-dep_Met_synth_activ_dom. [Graphical view]
PANTHER	PTHR21091:SF9. PTHR21091:SF9. 1 hit.
Pfam	PF02310. B12-binding. 1 hit. PF02607. B12-binding_2. 1 hit. PF02965. Met_synt_B12. 1 hit. PF00809. Pterin_bind. 1 hit. PF02574. S-methyl_trans. 1 hit. [Graphical view]
PIRSF	PIRSF000381. MetH. 1 hit.
SMART	SM01018. B12-binding_2. 1 hit. [Graphical view]
SUPFAM	SSF52242. Cbl-bd. 1 hit. SSF51717. DHP_synth_like. 1 hit. SSF56507. Met_synth_B12. 1 hit. SSF47644. Met_synth_Cbl-bd. 1 hit. SSF82282. S_methyl_trans. 1 hit.
TIGRFAMs	TIGR02082. metH. 1 hit.
PROSITE	PS50974. ADOMET_ACTIVATION. 1 hit. PS51332. B12_BINDING. 1 hit. PS51337. B12_BINDING_NTER. 1 hit. PS50970. HCY. 1 hit. PS50972. PTERIN_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METH_PSEAE

Accession

Primary (citable) accession number: Q9I2Q2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents