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METH_BOVIN
ID   METH_BOVIN              Reviewed;        1265 AA.
AC   Q4JIJ3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Methionine synthase;
DE            Short=MS;
DE            EC=2.1.1.13 {ECO:0000250|UniProtKB:Q9Z2Q4};
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE   AltName: Full=Cobalamin-dependent methionine synthase;
DE   AltName: Full=Vitamin-B12 dependent methionine synthase;
GN   Name=MTR;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Palin M.-F., Beaudry D., Charest R., Girard C.;
RT   "Interactions of folic acid-vitamin B12-methionine: effects on liver
RT   metabolism and production of dairy cows.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from
CC       methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound
CC       cob(I)alamin and methionine in the cytosol. MeCbl is an active form of
CC       cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis.
CC       Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl
CC       group from 5-methyltetrahydrofolate. The processing of cobalamin in the
CC       cytosol occurs in a multiprotein complex composed of at least MMACHC,
CC       MMADHC, MTRR (methionine synthase reductase) and MTR which may
CC       contribute to shuttle safely and efficiently cobalamin towards MTR in
CC       order to produce methionine. {ECO:0000250|UniProtKB:Q99707}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58199; EC=2.1.1.13;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z2Q4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11173;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z2Q4};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000250|UniProtKB:P13009};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P13009};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P13009};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
CC       {ECO:0000250|UniProtKB:Q99707}.
CC   -!- SUBUNIT: Monomer. Dimer. Forms a multiprotein complex with MMACHC,
CC       MMADHC AND MTRR. {ECO:0000250|UniProtKB:Q99707}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99707}.
CC   -!- DOMAIN: Modular enzyme with four functionally distinct domains. The
CC       isolated Hcy-binding domain catalyzes methyl transfer from free
CC       methylcobalamin to homocysteine. The Hcy-binding domain in association
CC       with the pterin-binding domain catalyzes the methylation of
CC       cob(I)alamin by methyltetrahydrofolate and the methylation of
CC       homocysteine. The B12-binding domain binds the cofactor. The AdoMet
CC       activation domain binds S-adenosyl-L-methionine. Under aerobic
CC       conditions cob(I)alamin can be converted to inactive cob(II)alamin.
CC       Reductive methylation by S-adenosyl-L-methionine and flavodoxin
CC       regenerates methylcobalamin (By similarity).
CC       {ECO:0000250|UniProtKB:P13009}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000305}.
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DR   EMBL; DQ084519; AAY86762.1; -; mRNA.
DR   RefSeq; NP_001025469.1; NM_001030298.1.
DR   AlphaFoldDB; Q4JIJ3; -.
DR   SMR; Q4JIJ3; -.
DR   STRING; 9913.ENSBTAP00000016262; -.
DR   PaxDb; Q4JIJ3; -.
DR   PRIDE; Q4JIJ3; -.
DR   GeneID; 280869; -.
DR   KEGG; bta:280869; -.
DR   CTD; 4548; -.
DR   eggNOG; KOG1579; Eukaryota.
DR   InParanoid; Q4JIJ3; -.
DR   OrthoDB; 731388at2759; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd02069; methionine_synthase_B12_BD; 1.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   Gene3D; 3.10.196.10; -; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   Gene3D; 3.20.20.330; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   InterPro; IPR033706; Met_synthase_B12-bd.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR   InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   Pfam; PF02965; Met_synt_B12; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF000381; MetH; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   SUPFAM; SSF56507; SSF56507; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   TIGRFAMs; TIGR02082; metH; 1.
DR   PROSITE; PS50974; ADOMET_ACTIVATION; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
DR   PROSITE; PS50970; HCY; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Cobalamin; Cobalt; Cytoplasm; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; Phosphoprotein;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN           1..1265
FT                   /note="Methionine synthase"
FT                   /id="PRO_0000251734"
FT   DOMAIN          19..338
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   DOMAIN          371..632
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   DOMAIN          662..759
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          772..907
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   DOMAIN          923..1265
FT                   /note="AdoMet activation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00346"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         382..384
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         449
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         470
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         537
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         579
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         585
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         591
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250|UniProtKB:Q99707"
FT   BINDING         709
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         782..786
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         785
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         830
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         834
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         886
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         974
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         1172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   BINDING         1227..1228
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P13009"
FT   MOD_RES         1264
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2Q4"
SQ   SEQUENCE   1265 AA;  140478 MW;  7E1E03AB95134529 CRC64;
     MAPTLQDLTP SAGMKKTLQD EIEAILQERI MVLDGGMGTM IQRHKLSEED FRGQEFKDHA
     RPLKGNNDIL SITQPNVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC
     SAGVARKAAE DISLQTGIKR YVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYKEQA
     KGLLDGGVDI LLIETIFDTA NAKAALFAVQ KLFEEEYVPR PVFISGTIVD KSGRTLSGQT
     GEAFVISVSH ADPLCIGLNC ALGAAEMRPF IETIGKCTTA YVLCYPNAGL PNTFGDYDET
     PHVMAMHLKD FAVDGLVNIV GGCCGTTPDH IREIAEAVKN CKPRVPPATV FEGHMLLSGL
     EPFRIGPYTN FVNIGERCNV AGSRRFAKLI MAGNYEEALS VAKMQVEMGA QVLDINMDDG
     MLDGPSAMTR FCNFIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD
     FLEKARKIKK FGAAVVVMAF DEEGQATETD PKIRVCTRAY HLLLKKLGFN PNDIIFDPNI
     LTIGTGMEEH NLYAVNFINA TKVIKETLPG AKVSGGLSNL SFSFRGMEAI REAMHGVFLY
     HAIKFGMDMG IVNAGSLPVY DDIHKELLQL CEDLIWNRDP EATEKLLHYA QTQGKGGKKV
     IQTDEWRNGP LEERLEYALV KGIEKYIIED TEEARLNQEK YPRPLNIIEG PLMNGMKIVG
     DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETKV LTGKIEDEDP YQGTIVLATV
     KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM
     IFVAKEMERL AIKIPLLIGG ATTSRTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN
     LKDEYFEEIL EEYEDIRQDH YESLKERRYL TLRQARENGF HIDWLSEPPP VKPTFLGTRV
     FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFDDK TVGEEAKKVY DDAQNMLQAL
     ISQKKLQARG VVGFWPAQSI QDDIHLYAEG AVPQASEPIA TFYGLRQQAE KDSASSDPYL
     CLSDFIAPLH SGIPDYLGLF AVACFGVEEL SKAYEEECDD YSSIMVKALG DRLAEAFAEE
     LHERARRELW GYCSGEQLAV ADLRRLRYEG IRPAPGYPSQ PDHTEKLTVW RLADVEQRTG
     IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQIED YASRKNMSVA EVEKWLGPIL
     GYDTD
 
 
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