ID   A5WD09_PSYWF            Unreviewed;      1272 AA.
AC   A5WD09;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   28-FEB-2018, entry version 84.
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   OrderedLocusNames=PsycPRwf_0595 {ECO:0000313|EMBL:ABQ93550.1};
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93550.1, ECO:0000313|Proteomes:UP000001993};
RN   [1] {ECO:0000313|EMBL:ABQ93550.1, ECO:0000313|Proteomes:UP000001993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93550.1,
RC   ECO:0000313|Proteomes:UP000001993};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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: 5-methyltetrahydrofolate + L-homocysteine =
CC       tetrahydrofolate + L-methionine. {ECO:0000256|PIRNR:PIRNR000381}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000381-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381-
CC       1};
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; CP000713; ABQ93550.1; -; Genomic_DNA.
DR   ProteinModelPortal; A5WD09; -.
DR   STRING; 349106.PsycPRwf_0595; -.
DR   EnsemblBacteria; ABQ93550; ABQ93550; PsycPRwf_0595.
DR   KEGG; prw:PsycPRwf_0595; -.
DR   eggNOG; ENOG4105C3R; Bacteria.
DR   eggNOG; COG0646; LUCA.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251409; -.
DR   KO; K00548; -.
DR   OMA; KYPRPLN; -.
DR   OrthoDB; POG091H030I; -.
DR   BioCyc; PSP349106:G12XP-603-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000001993; Chromosome.
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; -; 3.
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   4: Predicted;
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:UP000001993};
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,
KW   ECO:0000313|EMBL:ABQ93550.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001993};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000313|EMBL:ABQ93550.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1}.
FT   DOMAIN       47    367       Hcy-binding. {ECO:0000259|PROSITE:
FT                                PS50970}.
FT   DOMAIN      398    658       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      695    789       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      791    927       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      943   1272       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      879    880       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1238   1239       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   COILED      923    943       {ECO:0000256|SAM:Coils}.
FT   METAL       289    289       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       352    352       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       353    353       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       804    804       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     849    849       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     993    993       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING    1183   1183       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1187   1187       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1272 AA;  140989 MW;  EF63F634CBFEEDAB CRC64;
     MANCSHPEHN TKKDLPETAI KKGHNPDNFN LVPPAKFPFK EQQLTARQRI VEQLNQRILM
     LDGAMGTQIQ TFKLGESDYR GERFADFTQD VQGNNDLLVL TQPELIKSIH RDHLTAGADI
     IETNSFNGTQ ISMADYAMEH LVPEINKEAA RLAREVADEF TAQNPDKPRF VAGVIGPTSR
     TCSLSPDVND PAYRNVTFDE LVDNYTEALF ALIEGGIDLV LIETIFDTLN AKAAIFAVTG
     VFETIGFELP IMISGTITDA SGRTLSGQTA EAFYNSIRHA KPLSVGFNCA LGADALKPHI
     QTLSDIADTY ISAHPNAGLP NEFGEYDETP EQTAALLDGF GKSGLLNIVG GCCGTRPEHI
     KAIHDVMQKY PPRQIPTIAP ACRLSGLEPF TITKDSLFVN VGERTNVTGS KKFLRLIKTG
     EFTEALDVAR NQVDGGAQIV DINMDEGMLD SKGAMIHFLN LVAGEPDISR VPLMIDSSKW
     DIIEEGLKRT QGKSVVNSIS LKEGYDEFVK HAKLCMRYGA AVIVMAFDED GQADSYERKI
     QICQRSYDIL VNEVGFPSED IIFDPNIFAV ATGITEHNNY GADFINATRW ITDNLPNAMV
     SGGVSNVSFS FRGNPIREAI NAVFLYHAIQ AGLTMGIVNP AMLEVYDEIP KEARDAIEDV
     MLNRNQGESG QEATERLMTI AEAYVAGGKK NDGTIDLSWR EQSVEKRIEH ALVKGITTYI
     DEDTEEARLK YPKPLHVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KRAVAVLNPY
     IEAEKVEGEV KGKVVMATVK GDVHDIGKNI VGVVLGCNGY DVVDLGVMVP CDKILDTAIA
     EKADIIGLSG LITPSLDEMV YVAKQMQERG MTLPLMIGGA TTSKAHTAVK IEPNYQNDAV
     IYVSDASRSV GVVTKLLSQE HRVELLRETR EEYQKVRERL ANRKPKAAKL SYQESIEQGF
     KFDWDNYTPP VPNEQGQIIF DNYPIENLLP YIDWTPFFVS WGLVGKYPKI FDDEVVGAEA
     KDLFANAKAL MQTFIDEQLV TPKGVFKIMP ARRTDHDTVT VYDKEPSAGG QPTHVFEHLR
     QQSDKASGKP NYSLADFISP SEDYDDYLGG FTVSIVGAQE LSDSYKEAGD DYNAIMVQAL
     CDRLAEAFAE HLHELIRTKY WGYQPTEQLT NEELIKEKYV GIRPAPGYPA CPEHTEKGKL
     FDWLDTTNAI GTYLTESFAM WPASSVSGFY YSHPESTYFN VGKIDRDQLE DYAKRKDWDI
     KTAEKWLNPN LT
//