ID D4LYS9_9FIRM Unreviewed; 943 AA.
AC D4LYS9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=B12 binding domain./Pterin binding enzyme {ECO:0000313|EMBL:CBL22782.1};
GN ORFNames=CK5_13380 {ECO:0000313|EMBL:CBL22782.1};
OS Blautia obeum A2-162.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL22782.1, ECO:0000313|Proteomes:UP000008955};
RN [1] {ECO:0000313|EMBL:CBL22782.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL22782.1,
RC ECO:0000313|Proteomes:UP000008955};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus obeum A2-162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL22782.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL22782.1,
RC ECO:0000313|Proteomes:UP000008955};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; FP929054; CBL22782.1; -; Genomic_DNA.
DR AlphaFoldDB; D4LYS9; -.
DR KEGG; rob:CK5_13380; -.
DR PATRIC; fig|657314.3.peg.1145; -.
DR HOGENOM; CLU_311414_0_0_9; -.
DR Proteomes; UP000008955; Chromosome.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR CDD; cd02070; corrinoid_protein_B12-BD; 1.
DR Gene3D; 3.20.20.210; -; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 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; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR036594; Meth_synthase_dom.
DR InterPro; IPR000489; Pterin-binding_dom.
DR InterPro; IPR038071; UROD/MetE-like_sf.
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 Pfam; PF00809; Pterin_bind; 1.
DR SMART; SM01018; B12-binding_2; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 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.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..246
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 269..363
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 363..495
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 943 AA; 104588 MW; F88B1FAEB5A98C23 CRC64;
MIIIGEKLNG SIPSVAKAIA ERDADLIRER ARMQSEAGAT FLDVCASVEE DVEVETLKWM
IDIVQEVSDT PICVDSPSAK SCVAAIPFCK KPGLINSVSL EGDKIDTIFP VIADTDWECV
ALLCDNDGIP DSVERRMKIF FGIMEKAKQY GIAPDRLHID PLVVTLGTDQ TALTVFADCC
RRIKYEYPDI HITSGLSNIS FGLPVRKNIN QAFMVLAMNA GMDSAIVDPT NKNMIGMIYA
TNALLERDEY CLQYIDKFGN KVAGEDAQPA PASPLDEKMQ KVFKLTQDGK NKEIGQAVQE
ALDAGCDPTA ILNDAMIGAM AVVGDNFKKE IIFVPQMLAA ARAMKAGVEV LKPYLATGEA
GSAGTIILGT VAGDLHDIGK NLVGMMFESA GFEVIDLGVD VPIQTFIDEV NAHKEASIVA
LSALLTTTMP SLRDTVAALL KQPFRNRIKI MVGGAPISQE FADEIGADAY TEDAASAAEQ
AKKYAESGFC AKAAAGEFDD LPVEGAEVVQ EEVKEEAPKA EEKVSETPKF EKGAVDLSNI
QLPKPGEGYK LNWEATKEKF AAYWQHKNTG RPLMCVIARR PEVEQYSDGT PVEGGYLDQI
CQGKYYNMPE ELKWKDMEDK YQNAQRIVDR YRYFCDTHAF LGESFPNLNI DFGPGSVASY
LGSEIGFKED TVWFNKCLDS WDGVPKLEFD PENKWFKKHI QLAKDCKELA GDDFVVDMPD
LMENIDVLAS LRGAQDILFD LLDEPDMIGE RIQEVTDVYY EYYDRFYDII KDEEGGNAYT
VFQIWGPGRT VKLQCDFSAM MSPEDFRKYI QPSLREQSEK VDHVLYHLDG PAAIKHMDAL
MEIDGIDALQ WTSGDAGPDG TLPDWDVIYD KAIAAGKSIW VKVYSGEFED WIKNVDRIVK
KYGSHSLFLL FPEMSLEQAA YLLDYADKNW SDVKGTYVES LGR
//
