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Database: UniProt
Entry: Q2RII2_MOOTA
LinkDB: Q2RII2_MOOTA
Original site: Q2RII2_MOOTA 
ID   Q2RII2_MOOTA            Unreviewed;       556 AA.
AC   Q2RII2;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Cobalamin B12-binding protein {ECO:0000313|EMBL:ABC19757.1};
GN   OrderedLocusNames=Moth_1447 {ECO:0000313|EMBL:ABC19757.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC19757.1};
RN   [1] {ECO:0000313|EMBL:ABC19757.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC19757.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT   "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000232; ABC19757.1; -; Genomic_DNA.
DR   RefSeq; YP_430300.1; NC_007644.1.
DR   AlphaFoldDB; Q2RII2; -.
DR   STRING; 264732.Moth_1447; -.
DR   EnsemblBacteria; ABC19757; ABC19757; Moth_1447.
DR   KEGG; mta:Moth_1447; -.
DR   PATRIC; fig|264732.11.peg.1563; -.
DR   eggNOG; COG0407; Bacteria.
DR   eggNOG; COG5012; Bacteria.
DR   HOGENOM; CLU_489854_0_0_9; -.
DR   OrthoDB; 9780425at2; -.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR   CDD; cd02070; corrinoid_protein_B12-BD; 1.
DR   CDD; cd03465; URO-D_like; 1.
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; PTHR47099; METHYLCOBAMIDE:COM METHYLTRANSFERASE MTBA; 1.
DR   PANTHER; PTHR47099:SF1; METHYLCOBAMIDE:COM METHYLTRANSFERASE MTBA; 1.
DR   Pfam; PF02310; B12-binding; 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;
FT   DOMAIN          325..419
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51337"
FT   DOMAIN          419..550
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   556 AA;  59805 MW;  D79178899B37AAB0 CRC64;
     MRLIDLVNQS GRHLVFFIGS FPGAAMKGVT LKEVYFSASL QAETACYLAE RFQIDFIRPV
     TDLVVEAEAM GLKARYPDNG APVLVEHPIT GPEALANLNL PEPGRDGRLP INLEAIRLIK
     QRTDKPVIGS LTGPFTLAGA LCDPAGVAMK TITDPEFLHA LLAFCTRALK RYGEALLAAG
     ADILWISEPL GSLLSPAQFW QFSGRYIQEI FAAFPAMDIL HICGDTSYMI KEMLATGAQG
     LSLDSRVSLP VLATQMPEDV VLIGNIDPVG VMLEGSPQQV VKATANLLTA MLPFNNFIVS
     TGCTLPFEVP AANISAFVET ARNFPRLSPS QARLLLSLRR ALLEGDSEGV TTLTRKGLQL
     EVDAITILEG GLIQGINRAG ELYQQQKVFI PELLLISQAM YAGLEVIRPV LVQKRHGTRG
     EIVLGTVQGD LHDIGKNLVG LMLTANDYEV IDLGKDVAPE QFVEAVRACR PQVVGLSALT
     TTTMKSMEKT VRALKQGGQG EQVKVIVGGA PITPEFARRI GADAYAPDAA AAVTEVANLI
     DKVKEHQDGQ STTGVF
//
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