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Database: UniProt
Entry: Q9Z2Q4
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Original site: Q9Z2Q4 
ID   METH_RAT                Reviewed;        1253 AA.
AC   Q9Z2Q4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   01-OCT-2014, entry version 97.
DE   RecName: Full=Methionine synthase;
DE            EC=2.1.1.13;
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE   AltName: Full=Vitamin-B12 dependent methionine synthase;
DE            Short=MS;
GN   Name=Mtr;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=9972236; DOI=10.1271/bbb.62.2155;
RA   Yamada K., Tobimatsu T., Toraya T.;
RT   "Cloning, sequencing, and heterologous expression of rat methionine
RT   synthase cDNA.";
RL   Biosci. Biotechnol. Biochem. 62:2155-2160(1998).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
CC       cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
CC       methionine. Subsequently, remethylates the cofactor using
CC       methyltetrahydrofolate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine =
CC       tetrahydrofolate + L-methionine.
CC   -!- COFACTOR: Methylcobalamin (MeCBL). {ECO:0000250}.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Modular enzyme with four functionally distinct domains.
CC       The isolated Hcy-binding domain catalyzes methyl transfer from
CC       free methylcobalamin to homocysteine. The Hcy-binding domain in
CC       association with the pterin-binding domain catalyzes the
CC       methylation of cob(I)alamin by methyltetrahydrofolate and the
CC       methylation of homocysteine. The B12-binding domain binds the
CC       cofactor. The AdoMet activation domain binds S-adenosyl-L-
CC       methionine. Under aerobic conditions cob(I)alamin can be converted
CC       to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-
CC       methionine and flavodoxin regenerates methylcobalamin (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine
CC       synthase family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 AdoMet activation domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00346}.
CC   -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00666}.
CC   -!- SIMILARITY: Contains 1 B12-binding N-terminal domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00333}.
CC   -!- SIMILARITY: Contains 1 pterin-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00334}.
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DR   EMBL; AF034214; AAD05384.1; -; mRNA.
DR   PIR; T42376; T42376.
DR   RefSeq; NP_110491.1; NM_030864.1.
DR   UniGene; Rn.205061; -.
DR   ProteinModelPortal; Q9Z2Q4; -.
DR   SMR; Q9Z2Q4; 652-908, 914-1252.
DR   BioGrid; 249519; 1.
DR   IntAct; Q9Z2Q4; 1.
DR   STRING; 10116.ENSRNOP00000023973; -.
DR   PhosphoSite; Q9Z2Q4; -.
DR   PaxDb; Q9Z2Q4; -.
DR   PRIDE; Q9Z2Q4; -.
DR   GeneID; 81522; -.
DR   KEGG; rno:81522; -.
DR   UCSC; RGD:621283; rat.
DR   CTD; 4548; -.
DR   RGD; 621283; Mtr.
DR   eggNOG; COG1410; -.
DR   HOGENOM; HOG000251409; -.
DR   HOVERGEN; HBG006347; -.
DR   InParanoid; Q9Z2Q4; -.
DR   KO; K00548; -.
DR   PhylomeDB; Q9Z2Q4; -.
DR   UniPathway; UPA00051; UER00081.
DR   NextBio; 615041; -.
DR   PRO; PR:Q9Z2Q4; -.
DR   Genevestigator; Q9Z2Q4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR   GO; GO:0031419; F:cobalamin binding; TAS:RGD.
DR   GO; GO:0005542; F:folic acid binding; IDA:RGD.
DR   GO; GO:0008705; F:methionine synthase activity; IDA:RGD.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:RGD.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0050667; P:homocysteine metabolic process; IDA:RGD.
DR   GO; GO:0009086; P:methionine biosynthetic process; IDA:RGD.
DR   GO; GO:0006555; P:methionine metabolic process; IMP:RGD.
DR   GO; GO:0006479; P:protein methylation; IDA:RGD.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; IDA:RGD.
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   Gene3D; 3.40.50.280; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR000489; Pterin-binding.
DR   InterPro; IPR003726; S_MeTrfase.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
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; Complete proteome;
KW   Cytoplasm; Metal-binding; Methionine biosynthesis; Methyltransferase;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase;
KW   Zinc.
FT   CHAIN         1   1253       Methionine synthase.
FT                                /FTId=PRO_0000312902.
FT   DOMAIN        6    326       Hcy-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   DOMAIN      359    620       Pterin-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00334}.
FT   DOMAIN      650    747       B12-binding N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00666}.
FT   DOMAIN      760    895       B12-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00666}.
FT   DOMAIN      911   1253       AdoMet activation. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00346}.
FT   REGION      848    849       Cobalamin-binding. {ECO:0000250}.
FT   REGION     1215   1216       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       248    248       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       311    311       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       312    312       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       773    773       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000250}.
FT   BINDING     818    818       Cobalamin. {ECO:0000250}.
FT   BINDING     962    962       S-adenosyl-L-methionine. {ECO:0000250}.
FT   BINDING    1160   1160       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING    1164   1164       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000250}.
SQ   SEQUENCE   1253 AA;  139164 MW;  96BD40B796EBD75B CRC64;
     MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEENFQG QEFKDHSRPL KGNNDILSIT
     QPDVIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT
     LQTGVKRFVA GSLGPTNKTL SVSPSVERPD YRNITFDELV EAYQEQAKGL LDGGVDILLI
     ETIFDTANAK AALFALQKLF EENYASPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD
     PLCIGLNCAL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPA MMAMHLKDFA
     VDGLVNVVGG CCGSTPDHIR EIAEAVKNCK PRVPPDSVFE GHMLLSGLEP FRIGPYTNFV
     NIGERCNVAG SKKFAKLIMA GNYEEALSVA KVQVEMGAQV LDINMDDGML DGPSAMTKFC
     NFIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEEDFL EKARKIKKFG
     AAVVVMAFDE EGQATETDVK VSVCTRAYHL LVEKVGFNPN DIIFDPNILT IGTGMEEHNL
     YAINFIHATR VIKETLPGVR ISGGLSNLSF AFRGMDAIRE AMHGVFLYHA IKFGMDMGIV
     NAGSLPVYDD IHKDLLQLCE DLIWNRDAEA TEKLLRYAQT HGKGGKKVIQ TDEWRNGSIE
     ERLEYALVKG IEKHIVEDTE EARLNREKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ
     VIKSARVMKK AVGHLIPFME KEREEARVLN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV
     GVVLGCNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI
     KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYFEEILEE
     YEDIRQDHYE SLKERKYLPL SQARKHSFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY
     IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYED AQNMLSILIS RKKLRARGVV
     GFWPAQSVQD DIHLYAEGAV PQAAEPIATF YGLRQQAEKD SSSTDPYHCL SDFVAPLHSG
     VRDYLGLFAV ACFGVEELSK AYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY
     CGSEQLGVTD LRKLRYEGIR PAPGYPSQPD HTEKLTMWRL ANIEQATGIR LTESLAMAPA
     SAVSGLYFSN VKSKYFAVGK ISKDQIEDYA LRKNMSVAEV EKWLGPILGY DTD
//
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