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Database: UniProt
Entry: Q4VGS8_9BACT
LinkDB: Q4VGS8_9BACT
Original site: Q4VGS8_9BACT 
ID   Q4VGS8_9BACT            Unreviewed;       254 AA.
AC   Q4VGS8;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Methyltransferase/corrinoid binding protein {ECO:0000313|EMBL:AAY46984.1};
DE   Flags: Fragment;
GN   Name=cmuA {ECO:0000313|EMBL:AAY46984.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:AAY46984.1};
RN   [1] {ECO:0000313|EMBL:AAY46984.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16104855; DOI=10.1111/j.1462-5822.2005.00819.x;
RA   Borodina E., Cox M.J., McDonald I.R., Murrell J.C.;
RT   "Use of DNA-stable isotope probing and functional gene probes to
RT   investigate the diversity of methyl chloride-utilizing bacteria in soil.";
RL   Environ. Microbiol. 7:1318-1328(2005).
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DR   EMBL; AY934461; AAY46980.1; -; Genomic_DNA.
DR   EMBL; AY934465; AAY46984.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4VGS8; -.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.210; -; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   Pfam; PF01208; URO-D; 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   SUPFAM; SSF51726; UROD/MetE-like; 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:AAY46984.1};
KW   Transferase {ECO:0000313|EMBL:AAY46984.1}.
FT   DOMAIN          116..214
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51337"
FT   DOMAIN          216..254
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY46984.1"
FT   NON_TER         254
FT                   /evidence="ECO:0000313|EMBL:AAY46984.1"
SQ   SEQUENCE   254 AA;  27424 MW;  4064B8AB36BB7CDE CRC64;
     MDKTKQAIGG QISLMGTLSP YSTLMHGSTD DVRNEVKKIA AEVGYNGGCI VMPGCDIDWN
     IPEENLHAMI KQCSEIKYPM DVAALGDLSN VYLAGHPKHP GKRSSSAEGD QAIVEATTEI
     ADMNPTEEVN HYLVEAIMEY DGDKAIEWTN KGLERGMSPQ EIVFDGLSLG MKIVGDMYER
     NERFVTDMLK AAKTMDKAMP VLMPLLEASG GDGGPTGTVV VGLVRGNTQD IGKNLVCLML
     KANGFKVIDL GKNV
//
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