ID   A0A1J4NLC1_9GAMM        Unreviewed;      1228 AA.
AC   A0A1J4NLC1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   20-DEC-2017, entry version 11.
DE   SubName: Full=Methionine synthase {ECO:0000313|EMBL:OIJ39084.1};
GN   ORFNames=BK820_02005 {ECO:0000313|EMBL:OIJ39084.1};
OS   Acinetobacter sp. LCT-H3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1914307 {ECO:0000313|EMBL:OIJ39084.1, ECO:0000313|Proteomes:UP000186913};
RN   [1] {ECO:0000313|EMBL:OIJ39084.1, ECO:0000313|Proteomes:UP000186913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCT-H3 {ECO:0000313|EMBL:OIJ39084.1,
RC   ECO:0000313|Proteomes:UP000186913};
RA   Huang B.;
RT   "Draft genome sequence of strain LCT isolated from the Shenzhou X
RT   spacecraft of China.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|PIRSR:PIRSR000381-2};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OIJ39084.1}.
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DR   EMBL; MODX01000002; OIJ39084.1; -; Genomic_DNA.
DR   RefSeq; WP_071319950.1; NZ_MODX01000002.1.
DR   Proteomes; UP000186913; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase 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   CDD; cd02069; methionine_synthase_B12_BD; 1.
DR   Gene3D; 1.10.1240.10; -; 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   4: Predicted;
KW   Cobalamin {ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR000381-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186913};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00346};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00346};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}.
FT   DOMAIN        4    322       Hcy-binding. {ECO:0000259|PROSITE:
FT                                PS50970}.
FT   DOMAIN      353    614       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      651    745       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      747    883       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      899   1228       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      835    836       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1190   1191       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   METAL       244    244       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       307    307       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       308    308       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       760    760       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     805    805       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     949    949       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING    1135   1135       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1139   1139       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1228 AA;  135279 MW;  17BD4F3C873C5626 CRC64;
     MSTLATLKEL LAKRILIIDG AMGTMIQRHK LEEADYRGER FADWAYDLKG NNDLLVLTQP
     HIIQGIHEAY LEAGADIIET NTFNGTRVSM SDYHMEDLVP EINREAARLA KEACAKYSTP
     EKPRFVAGVI GPTSRTTSIS PNVNDPAFRN ITFDALKVDY IESTKALIEG GADIILIETV
     FDTLNAKAAI FAVKEVFKEI GYELPIMISG TITDASGRTL TGQTAEAFWN SMRHAEPISI
     GFNCALGADA MRPHVKTISD VADTFVSAHP NAGLPNAFGG YDETPEETAA FIKEFAESGL
     INITGGCCGT TPDHIRAIAQ AVEGIAPRQI PEIEPACRLS GLEPFNITKD SLFVNVGERT
     NVTGSKKFLR LIKEENFTEA LDVARQQVEA GAQIIDINMD EGMLDSQAAM VHFLNLIASE
     PDISRVPIML DSSKWEIIEA GLKCVQGKAV VNSISLKEGY DEFVERARLC RQYGAAVIVM
     AFDENGQADT AERKKEICKR SYDVLVNEVG FPSEDIIFDP NVFAVATGIE EHNNYGVDFI
     EATGWIKQNL PNAMISGGIS NVSFSFRGNE PVREAIHAVF LYHAIQKGLT MGIVNAGQLA
     IYDDIDAELK EAVEDVVLNR NQGESGQEAT EKLLTIAEKY RGQAGAQKAE ENLEWRNESV
     EKRLEYALVK GITTYIDQDT EEARLKSARP LDVIEGPLMA GMNVVGDLFG AGKMFLPQVV
     KSARVMKQAV AWLNPFIEAE KTQGEAKGKI LLATVKGDVH DIGKNIVGVV LGCNGYDIVD
     LGVMVPCEKI LQTAIDEKVD IIGLSGLITP SLDEMVFVAK EMQRKGFNIP LMIGGATTSK
     AHTAVKIAPQ YQNDGVFYTA DASRAVGVTT QLLSAEMKPQ LMADYAADYE KIRTRLANKQ
     PKAAKLSYKE SVENGFKIDF DKNAPVKPNF IGSQTFTNYP LETLVEYFDW TPFFISWSLA
     GKFPKILEDE VVGEAARDLY AQAQAMLKNI IDNKRFDARA TFSIYPANRT GSDTVAVTDE
     AGNVTHTFEH LRQQSDKVTG KANYSLADFI APKDVAQDYL GGFTVSIFGA EELSQEYKAK
     GDDYNAIMVQ ALGDRFAEAF AEHLHQRIRK EFWGYQPNES LDNEALIKEK YVGIRPAPGY
     PACPEHSEKA PLFDWLGTTE KMGTYLTSSF AMWPPSSVSG FYYANPETEY FNVGKISGDQ
     LEDYAKRKGW TLDEAKRWLA PNLDDSVV
//