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Database: UniProt
Entry: C6PZT4_9CLOT
LinkDB: C6PZT4_9CLOT
Original site: C6PZT4_9CLOT 
ID   C6PZT4_9CLOT            Unreviewed;       265 AA.
AC   C6PZT4;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Methionine synthase {ECO:0000313|EMBL:EET85241.1};
DE            EC=2.1.1.13 {ECO:0000313|EMBL:EET85241.1};
GN   ORFNames=CcarbDRAFT_4301 {ECO:0000313|EMBL:EET85241.1};
OS   Clostridium carboxidivorans P7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536227 {ECO:0000313|EMBL:EET85241.1, ECO:0000313|Proteomes:UP000004198};
RN   [1] {ECO:0000313|EMBL:EET85241.1, ECO:0000313|Proteomes:UP000004198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P7 {ECO:0000313|EMBL:EET85241.1,
RC   ECO:0000313|Proteomes:UP000004198};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT   "The draft genome of Clostridium carboxidivorans P7.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
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:EET85241.1}.
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DR   EMBL; ACVI01000100; EET85241.1; -; Genomic_DNA.
DR   RefSeq; WP_007063186.1; NZ_GG770693.1.
DR   AlphaFoldDB; C6PZT4; -.
DR   STRING; 536227.Ccar_13140; -.
DR   KEGG; cck:Ccar_13140; -.
DR   PATRIC; fig|536227.13.peg.2752; -.
DR   eggNOG; COG1410; Bacteria.
DR   OrthoDB; 358252at2; -.
DR   Proteomes; UP000004198; Unassembled WGS sequence.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EET85241.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004198};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EET85241.1}.
FT   DOMAIN          1..265
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   265 AA;  29402 MW;  373B304D60F26246 CRC64;
     MLIIGELINT SRKLIREAVE KKDGEYIKQV AKAQEEAGAT YIDVNCGTCI ETEVETMEWL
     VDNILQVTSL PLCIDSPNPL ALQAGLKKAA NGKLMINSIT FETPRWNAVL PLVKEFNTKI
     IALCIDDGGM PKTNEDRIRI ADSIITKLTG EGINIDDIYI DPLIKPVSAG QKNGIEVLQA
     IQNIMEGHPG VHTTCGLSNI SYSLPARKVL NTLFMVQTMA RGMDSYIMDP TNKEMRRALI
     ASQTLLGQDR FSRKFIKAFR EGLYD
//
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