(data stored in ACNUC7421 zone)

SWISSPROT: Q146I2_PARXL

ID   Q146I2_PARXL            Unreviewed;       905 AA.
AC   Q146I2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Methionine synthase {ECO:0000256|PIRNR:PIRNR000381};
DE            EC=2.1.1.13 {ECO:0000256|PIRNR:PIRNR000381};
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|PIRNR:PIRNR000381};
GN   ORFNames=Bxe_A4243 {ECO:0000313|EMBL:ABE28757.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28757.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28757.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28757.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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. {ECO:0000256|PIRNR:PIRNR000381}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-methionine;
CC         Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381,
CC         ECO:0000256|PIRSR:PIRSR000381-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1. {ECO:0000256|PIRNR:PIRNR000381}.
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DR   EMBL; CP000270; ABE28757.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_A4243; -.
DR   EnsemblBacteria; ABE28757; ABE28757; Bxe_A4243.
DR   KEGG; bxb:DR64_1919; -.
DR   KEGG; bxe:Bxe_A4243; -.
DR   eggNOG; ENOG4108J5I; Bacteria.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251409; -.
DR   KO; K00548; -.
DR   OMA; ADCIAMS; -.
DR   BioCyc; BXEN266265:BXE_RS01090-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
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   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   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; PS50972; PTERIN_BINDING; 1.
PE   4: Predicted;
DR   PRODOM; Q146I2.
DR   SWISS-2DPAGE; Q146I2.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Cobalamin {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-
KW   1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-1};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00346, ECO:0000313|EMBL:ABE28757.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00346, ECO:0000313|EMBL:ABE28757.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381}.
FT   DOMAIN       22    283       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      313    411       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      420    559       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      574    905       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      512    513       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION      872    873       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   COILED      558    578       {ECO:0000256|SAM:Coils}.
FT   METAL       433    433       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     478    478       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     624    624       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING     818    818       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING     822    822       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   905 AA;  100207 MW;  19A44BED6C7742E7 CRC64;
     MTDHTLRLAG LEPFNVTSGT LFINVGERTN VTGSKAFARM ILNDQFDDAI AVARQQVENG
     AQIIDVNMDE AMLDSKAAMV RFMNLIASEP DIARVPIMID SSKWEVIEAG LKCVQGKAIV
     NSISLKEGEE AFRHHANLIR RYGAAAVVMA FDEQGQADTF ERKTQICKRS YDFLVNEVGF
     PPEDIIFDPN IFAIATGIEE HNNYAVDFIN ATRWIKQNLP YAKVSGGVSN VSFSFRGNDP
     VREAIHTVFL YHAIQAGMDM GIVNAGQLGV YADLDPELRE RVEDVVLNRR EDGTDRLLEI
     ADKFKTGAAK KEENLEWRNQ PVEKRLSHAL VHGITNFIVE DTEEVRAKIA AEGGRPINVI
     EGPLMDGMNI VGDLFGQGKM FLPQVVKSAR VMKQAVAHLI PYIEEEKKQL AEAGADVRAK
     GKIVIATVKG DVHDIGKNIV SVVLQCNNFE VVNMGVMVSC NDILAKAKVE GADIIGLSGL
     ITPSLEEMAY VASEMQRDDY FRIKKIPLLI GGATTSRVHT AVKIAPHYEG PVVYVPDASR
     SVSVASSLLS DEGAAKYLDE LKSDYDRIRD QHANKKALPM VTLAEARANK TRVDWASYQP
     VKPKFIGRRV FRNFDLAELA TYIDWGPFFQ TWDLAGPYPA ILNDEIVGES ARRVFSDGKS
     MLARLIQGRW LQANGVIALL PANTVNDDDI EIYTDESRSE VALTWRNLRQ QSVRPVVDGV
     MRPNRSLADF IAPKDSGVAD YIGMFAVTAG LGVDVKEKQF EKDHDDYSAI MLKALADRFA
     EAFAEALHAR VRRDLWGYAN DETLSTDELI AEKYRGIRPA PGYPACPDHL VKRDMFNVLH
     ATEIGMSVTE SLAMLPAASV SGFYLAHPDS TYFSVGKIGQ DQLEDYARRM SLSKTDAERA
     LAPLL
//

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