ID   A5WD09_PSYWF            Unreviewed;      1272 AA.
AC   A5WD09;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   02-DEC-2020, entry version 105.
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., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., 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:
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:0000256|ARBA:ARBA00001700,
CC         ECO:0000256|PIRNR:PIRNR000381};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-ProRule:PRU00333};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000256|ARBA:ARBA00001956,
CC         ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-2};
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:0000256|ARBA:ARBA00005178, ECO:0000256|PIRNR:PIRNR000381}.
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. {ECO:0000256|PIRNR:PIRNR000381}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
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DR   EMBL; CP000713; ABQ93550.1; -; Genomic_DNA.
DR   STRING; 349106.PsycPRwf_0595; -.
DR   EnsemblBacteria; ABQ93550; ABQ93550; PsycPRwf_0595.
DR   KEGG; prw:PsycPRwf_0595; -.
DR   eggNOG; COG0646; Bacteria.
DR   eggNOG; COG1410; Bacteria.
DR   HOGENOM; CLU_004914_4_0_6; -.
DR   OMA; ADCIAMS; -.
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: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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR000381};
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00333};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167,
KW   ECO:0000256|PIRNR:PIRNR000381};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-ProRule:PRU00346,
KW   ECO:0000313|EMBL:ABQ93550.1}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PROSITE-ProRule:PRU00346, ECO:0000313|EMBL:ABQ93550.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          47..367
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   DOMAIN          398..658
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
FT   DOMAIN          695..789
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51337"
FT   DOMAIN          791..927
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          943..1272
FT                   /note="AdoMet activation"
FT                   /evidence="ECO:0000259|PROSITE:PS50974"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..880
FT                   /note="Cobalamin-binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT   REGION          1238..1239
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT   COILED          923..943
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        7..21
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           289
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   METAL           352
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   METAL           353
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00333"
FT   METAL           804
FT                   /note="Cobalt (cobalamin axial ligand)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-1"
FT   BINDING         849
FT                   /note="Cobalamin"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT   BINDING         993
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT   BINDING         1183
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT   BINDING         1187
FT                   /note="Cobalamin; via carbonyl oxygen"
FT                   /evidence="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
//