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Database: UniProt
Entry: Q9AJQ8
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Original site: Q9AJQ8 
ID   METH_ALIFS              Reviewed;        1226 AA.
AC   Q9AJQ8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   01-OCT-2014, entry version 67.
DE   RecName: Full=Methionine synthase;
DE            EC=2.1.1.13;
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE   AltName: Full=Methionine synthase, vitamin-B12 dependent;
DE            Short=MS;
GN   Name=metH;
OS   Aliivibrio fischeri (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RX   PubMed=11250084; DOI=10.1016/S0378-1119(01)00339-0;
RA   Kasai S., Yamazaki T.;
RT   "Identification of the cobalamin-dependent methionine synthase gene,
RT   metH, in Vibrio fischeri ATCC 7744 by sequencing using genomic DNA as
RT   a template.";
RL   Gene 264:281-288(2001).
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   -!- 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; AB039955; BAB39355.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9AJQ8; -.
DR   SMR; Q9AJQ8; 655-1225.
DR   PRIDE; Q9AJQ8; -.
DR   UniPathway; UPA00051; UER00081.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
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:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cobalamin; Cobalt; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; Repeat;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1   1226       Methionine synthase.
FT                                /FTId=PRO_0000204540.
FT   DOMAIN        7    327       Hcy-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   DOMAIN      358    619       Pterin-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00334}.
FT   DOMAIN      652    746       B12-binding N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00666}.
FT   DOMAIN      748    883       B12-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00666}.
FT   DOMAIN      899   1226       AdoMet activation. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00346}.
FT   REGION      836    837       Cobalamin-binding. {ECO:0000250}.
FT   REGION     1192   1193       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       249    249       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       312    312       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       313    313       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00333}.
FT   METAL       761    761       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000250}.
FT   BINDING     806    806       Cobalamin. {ECO:0000250}.
FT   BINDING     949    949       S-adenosyl-L-methionine. {ECO:0000250}.
FT   BINDING    1137   1137       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING    1141   1141       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000250}.
SQ   SEQUENCE   1226 AA;  136266 MW;  AF210E43E119E50C CRC64;
     MAGSNIKVQI EKQLSERILL IDGGMGTMIQ GYKFEEKDYR GGRFNQWHCD LKGNNDLLVL
     SQPQIIRDIH EAYLEAGADI LETNTFNATT IAMADYDMES LSEEINFEAA KLAREVADKW
     TEKTPNKPRY VAGVLGPTNR TCSISPDVND PGFRNVSFDE LVEAYSESTR ALIRGGSDLI
     LIETIFDTLN AKACSFAVES VFEELGITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV
     KPISFGLNCA LGPDELREYV SELSRISECY VSAHPNAGLP NAFGEYDLSP EDMAEHVAEW
     ASSGFLNLIG GCCGTTPEHI RQMALVVEGV KPRQLPELPV ACRLSGLEPL TIEKDSLFIN
     VGERTNVTGS ARFKRLIKEE LYDEALSVAQ EQVENGAQII DINMDEGMLD AEACMVRFLN
     LCASEPEISK VPVMVDSSKW EVIEAGLKCI QGKGIVNSIS LKEGKEKFVH QAKLIRRYGA
     AVIVMAFDEV GQADTRERKI EICTNAYNIL VDEVGFPPED IIFDPNIFAV ATGIDEHNNY
     AVDFIEAVGD IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IHAVFLYHCF KNGMDMGIVN
     AGQLEIYDNV PEDLREAVED VVLNRRDDST ERLLDIATEY LERAVGKVED KSALEWRDWP
     VEKRLEHSLV KGITEFIVED TEEARINAER PIEVIEGPLM DGMNVVGDLF GEGKMFLPQV
     VKSARVMKQA VAHLEPFINA SKEVGATNGK ILLATVKGDV HDIGKNIVGV VLQCNNYEII
     DLGVMVSCET ILKVAKEENV DIIGLSGLIT PSLDEMVHVA KEMERQGFDL PLLIGGATTS
     KAHTAVKIEQ NYSQPVVYVN NASRAVGVCT SLLSNELKPS FVEKLDIDYE RVREQHSRKQ
     PRTKPVTLEV ARANKVAIDW ASYTPPVPLK PGVHIFDNFD VSTLRNYIDW TPFFMTWSLV
     GKYPKILEHE EVGEEAKRLF KDANDLLDRV EKEGLLKARG MCALFPASSV GDDIEVYTDE
     SRTTVAKVLH NLRQQTEKPK GFNYCLSDYI APKESGKNDW IGGFAVTGGI GERELADEYK
     ANGDDYNAIM IQAVADRLAE AFAEYLHEKV RKEIWGYSPN ETLSNDDLIR EKYQGIRPAP
     GYPACPEHTE KGALWELMNV EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQQ
     DQAESYADRK GWNMLEAEKW LGPNLN
//
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