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MTMC2_METBA
ID   MTMC2_METBA             Reviewed;         217 AA.
AC   Q9P9L5;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Monomethylamine corrinoid protein 2;
DE            Short=MMCP 2;
GN   Name=mtmC2;
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RA   Srinivasan G., Burke S.A., Lo S.L., Krzycki J.A.;
RT   "Expression of two nearly identical copies of genes for monomethylamine
RT   methyltransferase and their cognate corrinoid proteins in Methanosarcina
RT   barkeri.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a methyl group carrier between MtmB and MtbA.
CC       {ECO:0000250}.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from methylamine.
CC   -!- SUBUNIT: Can form a complex with MtmB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF230870; AAF68951.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P9L5; -.
DR   SMR; Q9P9L5; -.
DR   UniPathway; UPA00643; -.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProt.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR012741; Corrinoid_p.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR02370; pyl_corrinoid; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
PE   3: Inferred from homology;
KW   Cobalt; Metal-binding; Methanogenesis; Repeat.
FT   CHAIN           1..217
FT                   /note="Monomethylamine corrinoid protein 2"
FT                   /id="PRO_0000216468"
FT   DOMAIN          1..91
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          93..217
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         106
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  23292 MW;  E7398F7D0CE32503 CRC64;
     MTNTEIFDKL RDAIVNQDVA GTPELCKEAL ALGIPALDII TKGLSVGMKI VGDKFEAAEI
     FLPQIMMSGK AMSNAMEVLT PELEKNKKEG DEAGLAITFV AEGDIHDIGH RLVTTMLGAN
     GFQIFDLGVD VLNETVVEEA AKHKGEKVLL VGSALMTTSM LGQKDLMDRL KEQKLRDSVK
     CMFGGAPVSD KWIEEIGADA TAENAAEAAK VALEVMK
 
 
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