UniProtKB - A0A5Q0JXB5 (A0A5Q0JXB5_9FLAO)
Protein
Methionine synthase
Gene
metH
Organism
Oceanihabitans sp. IOP_32
Status
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.UniRule annotation
Catalytic activityi
- (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionineUniRule annotationEC:2.1.1.13UniRule annotation
Cofactori
Protein has several cofactor binding sites:- Zn2+UniRule annotation
- methylcob(III)alaminUniRule annotation
: L-methionine biosynthesis via de novo pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetH route).UniRule annotationProteins known to be involved in this subpathway in this organism are:
- Methionine synthase (metH)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetH route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 426 | Cobalt (cobalamin axial ligand)UniRule annotation | 1 | |
Binding sitei | 471 | CobalaminUniRule annotation | 1 | |
Binding sitei | 614 | S-adenosyl-L-methionineUniRule annotation | 1 | |
Binding sitei | 800 | S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 804 | Cobalamin; via carbonyl oxygenUniRule annotation | 1 |
GO - Molecular functioni
- cobalamin binding Source: UniProtKB-UniRule
- methionine synthase activity Source: UniProtKB-UniRule
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- methylation Source: UniProtKB-KW
- pteridine-containing compound metabolic process Source: InterPro
Keywordsi
Molecular function | MethyltransferaseUniRule annotationImported, Transferase |
Biological process | Amino-acid biosynthesis, Methionine biosynthesisUniRule annotation |
Ligand | CobalaminUniRule annotation, Cobalt, Metal-bindingUniRule annotation, S-adenosyl-L-methionineUniRule annotationARBA annotation, ZincUniRule annotation |
Enzyme and pathway databases
UniPathwayi | UPA00051;UER00081 |
Names & Taxonomyi
Protein namesi | Recommended name: Methionine synthaseUniRule annotation (EC:2.1.1.13UniRule annotation)Alternative name(s): 5-methyltetrahydrofolate--homocysteine methyltransferaseUniRule annotation |
Gene namesi | Name:metHImported ORF Names:FEZ18_10030Imported |
Organismi | Oceanihabitans sp. IOP_32Imported |
Taxonomic identifieri | 2529032 [NCBI] |
Taxonomic lineagei | Bacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Oceanihabitans › unclassified Oceanihabitans |
Proteomesi |
|
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 323 – 406 | B12-binding N-terminalInterPro annotationAdd BLAST | 84 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 501 – 502 | Cobalamin-bindingUniRule annotation | 2 | |
Regioni | 855 – 856 | S-adenosyl-L-methionine bindingUniRule annotation | 2 |
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.UniRule annotation
Sequence similaritiesi
Belongs to the vitamin-B12 dependent methionine synthase family.ARBA annotation
Keywords - Domaini
RepeatARBA annotationFamily and domain databases
CDDi | cd02069, methionine_synthase_B12_BD, 1 hit |
Gene3Di | 1.10.1240.10, 1 hit 3.10.196.10, 1 hit 3.20.20.20, 1 hit |
InterProi | View protein in InterPro IPR003759, Cbl-bd_cap IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf IPR011005, Dihydropteroate_synth-like IPR033706, Met_synthase_B12-bd IPR011822, MetH IPR036594, Meth_synthase_dom IPR000489, Pterin-binding_dom IPR004223, VitB12-dep_Met_synth_activ_dom IPR037010, VitB12-dep_Met_synth_activ_sf |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit PF02607, B12-binding_2, 1 hit PF02965, Met_synt_B12, 1 hit PF00809, Pterin_bind, 1 hit |
PIRSFi | PIRSF000381, MetH, 1 hit |
SMARTi | View protein in SMART SM01018, B12-binding_2, 1 hit |
SUPFAMi | SSF47644, SSF47644, 1 hit SSF51717, SSF51717, 1 hit SSF52242, SSF52242, 1 hit SSF56507, SSF56507, 1 hit |
TIGRFAMsi | TIGR02082, metH, 1 hit |
i Sequence
Sequence statusi: Complete.
A0A5Q0JXB5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKVKQTKYMR LSGLEPLVLN ENSNFINVGE RTNVAGSRKF LRLIKEENYD
60 70 80 90 100
EALDIARHQV DGGAQILDVN FDDGLIDGKE AMIRFLNLIA AEPDICKVPI
110 120 130 140 150
MIDSSKWEII EAGLQVVQGK CVVNSISLKE GEANFIWEAK QIKRYGAAVI
160 170 180 190 200
VMAFDEVGQA DTYERRIEIA KRSYDILVDK VGFPSEDIIF DLNIFPVATG
210 220 230 240 250
MEEHRRNAID FIEATRWVRE NLPNVSVSGG VSNVSFSFRG NNGVREAMHS
260 270 280 290 300
VFLYHAIQAG MNIGIVNPAL LEVYDDIPKD LLEHVEDVIL DRRDDATERL
310 320 330 340 350
LDFAETVKGS KKEAGADLSW RENPLQDRIT HALVKGIDSY IVEDVEQARQ
360 370 380 390 400
EANSPIDVIE GHLMTGMNVV GDLFGAGKMF LPQVVKSARV MKKAVGYLNP
410 420 430 440 450
FIEAAKTDKQ EPVGKILMAT VKGDVHDIGK NIVSVVLACN NYEIVDLGVM
460 470 480 490 500
VPPEKIIETA IRERVDAIGL SGLITPSLDE MVYLAKEMQR NNLELPLLIG
510 520 530 540 550
GATTSKAHTA VKIDTQYNNA VVHVNDASRA VTVVGDLLNK KSSQDYVAKL
560 570 580 590 600
KKDYDEFRTK FLKRGKEKSY ISIEEARKRK YKIDWNATEI VKPNTLGIQV
610 620 630 640 650
LEQLSLKELL PFIDWSPFFR SWDLHGKFPD ILTDKVVGEQ ATIMYEEAQR
660 670 680 690 700
MIKVIIAKQL FKPKAIFGLF EANSIHHDDI SVIRKGKEIA VFRTLRQQLK
710 720 730 740 750
KREGIPNHAL ADFIAPKDSG KTDYLGLFSV GIFGAQELAE SYKLKDDDYN
760 770 780 790 800
AIMAQAIADR FAEALAEYLH KQIRMKHWGY AANENLTNDD LIKESYKGIR
810 820 830 840 850
PAPGYPACPD HLEKETIWEL LDVEKRIGIS LTESLAMWPA AAVSGYYFAN
860 870 880 890
PEAKYFGLGK ITDDQVTDYA KRKGITKAKA RKWLHANIAE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP040813 Genomic DNA Translation: QFZ55105.1 |
Genome annotation databases
KEGGi | oci:FEZ18_10030 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP040813 Genomic DNA Translation: QFZ55105.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Genome annotation databases
KEGGi | oci:FEZ18_10030 |
Enzyme and pathway databases
UniPathwayi | UPA00051;UER00081 |
Family and domain databases
CDDi | cd02069, methionine_synthase_B12_BD, 1 hit |
Gene3Di | 1.10.1240.10, 1 hit 3.10.196.10, 1 hit 3.20.20.20, 1 hit |
InterProi | View protein in InterPro IPR003759, Cbl-bd_cap IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf IPR011005, Dihydropteroate_synth-like IPR033706, Met_synthase_B12-bd IPR011822, MetH IPR036594, Meth_synthase_dom IPR000489, Pterin-binding_dom IPR004223, VitB12-dep_Met_synth_activ_dom IPR037010, VitB12-dep_Met_synth_activ_sf |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit PF02607, B12-binding_2, 1 hit PF02965, Met_synt_B12, 1 hit PF00809, Pterin_bind, 1 hit |
PIRSFi | PIRSF000381, MetH, 1 hit |
SMARTi | View protein in SMART SM01018, B12-binding_2, 1 hit |
SUPFAMi | SSF47644, SSF47644, 1 hit SSF51717, SSF51717, 1 hit SSF52242, SSF52242, 1 hit SSF56507, SSF56507, 1 hit |
TIGRFAMsi | TIGR02082, metH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | A0A5Q0JXB5_9FLAO | |
Accessioni | A0A5Q0JXB5Primary (citable) accession number: A0A5Q0JXB5 | |
Entry historyi | Integrated into UniProtKB/TrEMBL: | April 22, 2020 |
Last sequence update: | April 22, 2020 | |
Last modified: | February 10, 2021 | |
This is version 5 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Unreviewed (UniProtKB/TrEMBL) |