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Q9I2Q2

- METH_PSEAE

UniProt

Q9I2Q2 - METH_PSEAE

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Protein

Methionine synthase

Gene

metH

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi254 – 2541ZincPROSITE-ProRule annotation
Metal bindingi317 – 3171ZincPROSITE-ProRule annotation
Metal bindingi318 – 3181ZincPROSITE-ProRule annotation
Metal bindingi765 – 7651Cobalt (cobalamin axial ligand)By similarity
Binding sitei810 – 8101CobalaminBy similarity
Binding sitei954 – 9541S-adenosyl-L-methionineBy similarity
Binding sitei1142 – 11421S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1146 – 11461Cobalamin; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. methionine synthase activity Source: UniProtKB-EC
  3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. pteridine-containing compound metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

UniPathwayiUPA00051; UER00081.

Names & Taxonomyi

Protein namesi
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 namesi
Name:metH
Ordered Locus Names:PA1843
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA1843.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12341234Methionine synthasePRO_0000287780Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi208964.PA1843.

Structurei

3D structure databases

ProteinModelPortaliQ9I2Q2.
SMRiQ9I2Q2. Positions 19-646, 658-1233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 332321Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini363 – 624262Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini655 – 74995B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini752 – 888137B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini904 – 1234331AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni840 – 8412Cobalamin-bindingBy similarity
Regioni1197 – 11982S-adenosyl-L-methionine bindingBy similarity

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
Contains 1 B12-binding domain.PROSITE-ProRule annotation
Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1410.
HOGENOMiHOG000251409.
InParanoidiQ9I2Q2.
KOiK00548.
OMAiLTEHYAM.
OrthoDBiEOG6091CH.
PhylomeDBiQ9I2Q2.

Family and domain databases

Gene3Di1.10.1240.10. 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.
InterProiIPR003759. 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]
PfamiPF02310. 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]
PIRSFiPIRSF000381. MetH. 1 hit.
SMARTiSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsiTIGR02082. metH. 1 hit.
PROSITEiPS50974. 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]

Sequencei

Sequence statusi: Complete.

Q9I2Q2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSPLTDRSA RLQALQHALR ERILILDGGM GTMIQSYKLE EADYRGERFA
60 70 80 90 100
DWPSDVKGNN DLLLLSRPDV IQAIEKAYLD AGADILETNT FNATQVSQAD
110 120 130 140 150
YGMQSLAYEL NVEGARLARQ VADAKTAETP DKPRFVAGVL GPTSRTCSIS
160 170 180 190 200
PDVNNPGYRN VTFDELVENY VEATRGLIEG GADLILIETI FDTLNAKAAI
210 220 230 240 250
FAVQGVFEEL GVELPIMISG TITDASGRTL SGQTTEAFWN SVRHARPISV
260 270 280 290 300
GLNCALGAKE LRPYIEELST KADTHVSAHP NAGLPNAFGE YDESPAEMAV
310 320 330 340 350
VVEEFAAAGF LNIVGGCCGT TPAHIEAIAK AVAKYPPRAI PEIPRACRLS
360 370 380 390 400
GLEPFTIDRS SLFVNVGERT NITGSAKFAR LIREENYAEA LEVAQQQVEA
410 420 430 440 450
GAQVIDINMD EGMLDSKAAM VTFLNLIASE PDISRVPIMI DSSKWEVIEA
460 470 480 490 500
GLKCIQGKGI VNSISMKEGV EAFKHHARLC KRYGAAVVVM AFDEDGQADT
510 520 530 540 550
QARKEEICKR SYDILVDEVG FPPEDIIFDA NIFAIATGIE EHNNYAVDFI
560 570 580 590 600
NACAYIRDNL PYALSSGGVS NVSFSFRGNN PVREAIHSVF LYYAIRNGLT
610 620 630 640 650
MGIVNAGQLE IYDEIPKALR DRVEDVVLNR TPEATEALLA IADDYKGGGA
660 670 680 690 700
VKEAEDEEWR SYSVEKRLEH ALVKGITTWI VEDTEECRQQ CARPIEVIEG
710 720 730 740 750
PLMSGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAHLIPF IEAEKGDKPE
760 770 780 790 800
AKGKILMATV KGDVHDIGKN IVGVVLGCNG YDVVDLGVMV PAEKILQTAI
810 820 830 840 850
AEKCDIIGLS GLITPSLDEM VHVAKEMQRQ NFQLPLMIGG ATTSKAHTAV
860 870 880 890 900
KIDPQYSNDA VVYVTDASRA VGVATSLLSK ELKADYVART RADYAVVRER
910 920 930 940 950
TANRSARTER LSYEQAIANK PAFDWAGYQA PTPSFTGVRV LDEIDLAVLA
960 970 980 990 1000
EYIDWTPFFI SWDLAGKYPR ILTDEVVGEA ATSLFNDAQA MLKKLIDEKL
1010 1020 1030 1040 1050
IKARAVFGFW PANQVEHDDL EVYGADGETL ATLHHLRQQT IKPDGKPNLS
1060 1070 1080 1090 1100
LADFVAPKES GVRDYIGGFI TTAGIGAEEV AKAYEAKGDD YNSIMVKALA
1110 1120 1130 1140 1150
DRLAEACAEW LHERVRKEYW GYARDEHLDN EALIKEQYVG IRPAPGYPAC
1160 1170 1180 1190 1200
PDHTEKGTLF ELLDPQGLSG VSLTEHYAMF PAAAVSGWYF AHPQAQYFAV
1210 1220 1230
GKIDKDQVER YSQRKGQEAS VSERWLAPNL GYDD
Length:1,234
Mass (Da):135,063
Last modified:March 1, 2001 - v1
Checksum:i9877F8AC8BEF44ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG05232.1.
PIRiE83415.
RefSeqiNP_250534.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG05232; AAG05232; PA1843.
GeneIDi880631.
KEGGipae:PA1843.
PATRICi19838071. VBIPseAer58763_1916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG05232.1 .
PIRi E83415.
RefSeqi NP_250534.1. NC_002516.2.

3D structure databases

ProteinModelPortali Q9I2Q2.
SMRi Q9I2Q2. Positions 19-646, 658-1233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA1843.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG05232 ; AAG05232 ; PA1843 .
GeneIDi 880631.
KEGGi pae:PA1843.
PATRICi 19838071. VBIPseAer58763_1916.

Organism-specific databases

PseudoCAPi PA1843.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
InParanoidi Q9I2Q2.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG6091CH.
PhylomeDBi Q9I2Q2.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .

Family and domain databases

Gene3Di 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.
InterProi 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 ]
Pfami 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 ]
PIRSFi PIRSF000381. MetH. 1 hit.
SMARTi SM01018. B12-binding_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsi TIGR02082. metH. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiMETH_PSEAE
AccessioniPrimary (citable) accession number: Q9I2Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

L-homocysteine is bound via the zinc atom.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3