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Database: UniProt
Entry: A0A259UK37_9FIRM
LinkDB: A0A259UK37_9FIRM
Original site: A0A259UK37_9FIRM 
ID   A0A259UK37_9FIRM        Unreviewed;       210 AA.
AC   A0A259UK37;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 10.
DE   SubName: Full=Methionine synthase {ECO:0000313|EMBL:OZC18523.1};
DE            EC=2.1.1.13 {ECO:0000313|EMBL:OZC18523.1};
GN   Name=metH_12 {ECO:0000313|EMBL:OZC18523.1};
GN   ORFNames=SPACI_33890 {ECO:0000313|EMBL:OZC18523.1};
OS   Sporomusa acidovorans DSM 3132.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC18523.1, ECO:0000313|Proteomes:UP000216052};
RN   [1] {ECO:0000313|EMBL:OZC18523.1, ECO:0000313|Proteomes:UP000216052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC18523.1,
RC   ECO:0000313|Proteomes:UP000216052};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZC18523.1}.
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DR   EMBL; LSLL01000068; OZC18523.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259UK37; -.
DR   STRING; 112900.SAMN04488499_101259; -.
DR   Proteomes; UP000216052; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02070; corrinoid_protein_B12-BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF47644; Methionine synthase domain; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:OZC18523.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216052};
KW   Transferase {ECO:0000313|EMBL:OZC18523.1}.
FT   DOMAIN          1..88
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51337"
FT   DOMAIN          88..210
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   210 AA;  21952 MW;  0DFB270BD1695E57 CRC64;
     MANFENLAQS VISGREGQVK EQVQALVDSG ASPLAIISEG LIAGMNIVGA SFKKGDMFVP
     EVLRSAKAMS AGIEMVKPLI ADKDMPSLGT VVIGAVQGDL HDIGKNLVTM MLEGGGFKVI
     DLGIDISSEK FIVAVKEHNA KIVAMAALLT TTMPAMKETI DLLAKEGLRD KVKVIIGGAP
     ITEDFANQIG ADGYAPDAAV AVDLCKEWVA
//
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