MTMC1_METBA
ID MTMC1_METBA Reviewed; 217 AA.
AC O30641;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Monomethylamine corrinoid protein 1;
DE Short=MMCP 1;
GN Name=mtmC1;
OS Methanosarcina barkeri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2208;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-28.
RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX PubMed=9642198; DOI=10.1128/jb.180.13.3432-3440.1998;
RA Burke S.A., Lo S.L., Krzycki J.A.;
RT "Clustered genes encoding the methyltransferases of methanogenesis from
RT monomethylamine.";
RL J. Bacteriol. 180:3432-3440(1998).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX PubMed=7635826; DOI=10.1128/jb.177.15.4410-4416.1995;
RA Burke S.A., Krzycki J.A.;
RT "Involvement of the 'A' isozyme of methyltransferase II and the 29-
RT kilodalton corrinoid protein in methanogenesis from monomethylamine.";
RL J. Bacteriol. 177:4410-4416(1995).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX PubMed=9195968; DOI=10.1074/jbc.272.26.16570;
RA Burke S.A., Krzycki J.A.;
RT "Reconstitution of monomethylamine:coenzyme M methyl transfer with a
RT corrinoid protein and two methyltransferases purified from Methanosarcina
RT barkeri.";
RL J. Biol. Chem. 272:16570-16577(1997).
RN [4]
RP MASS SPECTROMETRY.
RX PubMed=12029132; DOI=10.1126/science.1069556;
RA Hao B., Gong W., Ferguson T.K., James C.M., Krzycki J.A., Chan M.K.;
RT "A new UAG-encoded residue in the structure of a methanogen
RT methyltransferase.";
RL Science 296:1462-1466(2002).
CC -!- FUNCTION: Acts as a methyl group carrier between MtmB and MtbA.
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from methylamine.
CC -!- SUBUNIT: Can form a complex with MtmB.
CC -!- MASS SPECTROMETRY: Mass=23066; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12029132};
CC -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC {ECO:0000305}.
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DR EMBL; AF013713; AAC38633.1; -; Genomic_DNA.
DR PDB; 3EZX; X-ray; 2.56 A; A=2-216.
DR PDBsum; 3EZX; -.
DR AlphaFoldDB; O30641; -.
DR SMR; O30641; -.
DR PRIDE; O30641; -.
DR BioCyc; MetaCyc:MON-12209; -.
DR UniPathway; UPA00643; -.
DR EvolutionaryTrace; O30641; -.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0043852; F:monomethylamine methyltransferase activity; IDA:MENGO.
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 1: Evidence at protein level;
KW 3D-structure; Cobalt; Direct protein sequencing; Metal-binding;
KW Methanogenesis; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9642198"
FT CHAIN 2..217
FT /note="Monomethylamine corrinoid protein 1"
FT /id="PRO_0000216467"
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"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 62..83
FT /evidence="ECO:0007829|PDB:3EZX"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:3EZX"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:3EZX"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3EZX"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3EZX"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:3EZX"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:3EZX"
SQ SEQUENCE 217 AA; 23198 MW; CEE5A4011CBBC1BA CRC64;
MANQEIFDKL RDAIVNQNVA GTPELCKEAL AAGVPALDII TKGLSVGMKI VGDKFEAAEI
FLPQIMMSGK AMSNAMEVLT PELEKNKKEG EEAGLAITFV AEGDIHDIGH RLVTTMLGAN
GFQIVDLGVD VLNENVVEEA AKHKGEKVLL VGSALMTTSM LGQKDLMDRL NEEKLRDSVK
CMFGGAPVSD KWIEEIGADA TAENAAEAAK VALEVMK
