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Database: UniProt
Entry: A0A0B2K4F5_9FIRM
LinkDB: A0A0B2K4F5_9FIRM
Original site: A0A0B2K4F5_9FIRM 
ID   A0A0B2K4F5_9FIRM        Unreviewed;       221 AA.
AC   A0A0B2K4F5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cobalamin-binding protein {ECO:0000313|EMBL:KHM52962.1};
GN   ORFNames=NZ47_01625 {ECO:0000313|EMBL:KHM52962.1};
OS   Anaerovibrio lipolyticus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Anaerovibrio.
OX   NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM52962.1, ECO:0000313|Proteomes:UP000030993};
RN   [1] {ECO:0000313|EMBL:KHM52962.1, ECO:0000313|Proteomes:UP000030993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5S {ECO:0000313|EMBL:KHM52962.1,
RC   ECO:0000313|Proteomes:UP000030993};
RX   PubMed=23950883;
RA   Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA   Scollan N.D., Huws S.A., Newbold C.J.;
RT   "Identification and characterization of three novel lipases belonging to
RT   families II and V from Anaerovibrio lipolyticus 5ST.";
RL   PLoS ONE 8:E69076-E69076(2013).
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:KHM52962.1}.
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DR   EMBL; JSCE01000027; KHM52962.1; -; Genomic_DNA.
DR   RefSeq; WP_039205959.1; NZ_JSCE01000027.1.
DR   AlphaFoldDB; A0A0B2K4F5; -.
DR   STRING; 82374.NZ47_01625; -.
DR   eggNOG; COG5012; Bacteria.
DR   Proteomes; UP000030993; 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:UniProt.
DR   CDD; cd02070; corrinoid_protein_B12-BD; 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   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   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF47644; Methionine synthase domain; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030993}.
FT   DOMAIN          1..91
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51337"
FT   DOMAIN          91..221
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   221 AA;  23730 MW;  F6C2437139BBE4FF CRC64;
     MEKEELLRQI ADAVVEMEED TVEELAQQSL TAGIDAYETI DLGLAKGMER AGQLFDEEEY
     FVPELLMCSD AMNVGIDVLK PHLKSENVSK KGKVVIGVVE GDTHDIGKNL VRLMMETGGF
     EVLDLGRDIP PAEFVSKAEE YGADIIGIAT LMTTTMPGMK EVVDILADKG IRDKFKVIVG
     GGPISPAFAK KIGADGYARN AADAVKVAEK LLSNTDLALG A
//
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