ID R5AM69_9CLOT Unreviewed; 485 AA.
AC R5AM69;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=B12 binding domain./Pterin binding enzyme {ECO:0000313|EMBL:CCX41892.1};
GN ORFNames=BN454_01193 {ECO:0000313|EMBL:CCX41892.1};
OS Clostridium sp. CAG:1024.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262770 {ECO:0000313|EMBL:CCX41892.1, ECO:0000313|Proteomes:UP000017946};
RN [1] {ECO:0000313|EMBL:CCX41892.1, ECO:0000313|Proteomes:UP000017946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1024 {ECO:0000313|Proteomes:UP000017946};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX41892.1}.
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DR EMBL; CAWJ010000160; CCX41892.1; -; Genomic_DNA.
DR AlphaFoldDB; R5AM69; -.
DR STRING; 1262770.BN454_01193; -.
DR Proteomes; UP000017946; 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 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 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 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:UP000017946};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..253
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 267..360
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 359..485
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 485 AA; 51231 MW; E729D8CCA8E50E8A CRC64;
MLWIGEKLNG AVPSIAAAIA EGDGKMIERI ARAQAEAGAD FLDVSAATTG GSAATTAEEL
QALRFLIENA EKGAALPLCI DSPDPMAVVQ AMAFCSRPGL LNSVSMEGRK ADIIFPAMQG
NAWRAVALLS DDRGTPDSVE ERMAVLERLL ECAGQYGIEE ERLYVDPLVE ALPVSPNAFL
KFAACARAVK AAHPRLHVLG GMSNISYGLP ERRRLYGAFL KLAAEAGVDA IISDPRSKND
PVDPVAEAAL LGRDPGCRAY IAACTHRDAE ICEQTPAGLL MSAVEQGNAE RGGRLAEEAL
RAGAAPLALL DGMTETMAEL GRRFAAGTVY IPELIMAAKT MQAATEVLKP LLGENTARLG
TVVIGTVMGD VHDIGKNLVA MMLEGAGFTV IDLGTDVYTE DFIEAVEQHP ETKIIALSAL
LTTTMPAMRD TVRALRQEPC CRGIRIMVGG APVTETFAQQ IGADAYTQNA AMAAERAREL
IAQGG
//
