ID A0A0J1G8H7_9FIRM Unreviewed; 951 AA.
AC A0A0J1G8H7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=B12-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHS_2312 {ECO:0000313|EMBL:KLU71598.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71598.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU71598.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU71598.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU71598.1}.
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DR EMBL; JNGB01000020; KLU71598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1G8H7; -.
DR PATRIC; fig|1504536.3.peg.2666; -.
DR Proteomes; UP000036477; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000036477};
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 951 AA; 105132 MW; F90785E4014330CC CRC64;
MIIIGEKLNG SIPAVAKAIA SRDAQLIKER AKLQADAGAD FLDVCASVEE EEEIETLRWM
IEQVQEVTDT PICVDSPSAK SCIGALPFCK RPGLLNSVSL EGDKIDTIFP LIADTNWECV
ALLCDNEGIP DSVERRMKVF HGIMEKAREY GIDPSRLHID PLVVTLSTDE TALQVFAKCC
RLIKEEYPDI HITSGLSNIS YGLPVRKNIN QAFMVLAMNA GMDSAIVDPT NKNMIGMIYA
TTALLGKDEF CLNYIKEFQE KKETGVDINE LTKDMIPEMK DVFLATQHGK NKEIGSLVQS
ALAAGCDPVD VLNDGMIGAM AVVGDHFKKE IIFVPQMLSA ARAMKAGVEV LKPHLATGGA
GSAGKMILGT VAGDLHDIGK NLVGMMIESA GFEVIDLGVD VPIEVFIKEI EEHPDVTIVG
LSALLTTTMP SLRNTVAALN NAPFRSRIKI MVGGAPISQA FADEIGADAY TADAAEAADK
AKELAKAGTG SVPVSRTAVI KSIAGEDGSV TAGAERVEAE RFKAESVGAE RVEAETENVL
SQLAGIKFTG VSPAVSGIPY KENMDAVKEK FTNYWKHRNI GRPLMCVIAR KPEMEAFSDG
TPVEGGYLDQ ICQGKYYNMP EELKWKDMED KYQNPEQIVA RYRYFCETHD FLGESFPNLN
VDFGPGSLAA YLGSDIGFKE DTVWFKPCLD SWDGVSRFKF DPENEWYKKH IKLVTRCREL
AGDDFYVDMP DLMENIDVLA SLRGAQEILF DMLDEPETIG ERIGEITNLY YDYYNRFYDV
IKDEKGGNAY TVFQIWGPGR TVKLQCDFSA MMSPDDFRQY IQPSLKAQAD QADYVLYHLD
GPAAIKHLDA LMEIEGIDAL QWTSGDAGPD GTLPDWDVIY DKAIAAGKSI WVKVYSGNFE
DWIKNVDRLV QKYGSHSLFL LFPEMSRRQA DTLLQYAEEH WKDVPGTFYV R
//
