MTAC_METBF
ID MTAC_METBF Reviewed; 258 AA.
AC Q46EH4; P94920;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Methanol--corrinoid protein;
DE AltName: Full=Methanol:corrinoid methyltransferase 1 subunit of 27 kDa;
DE Short=MT1 subunit 27 kDa;
GN Name=mtaC; OrderedLocusNames=Mbar_A0740;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-60, AND FUNCTION.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=9057830; DOI=10.1111/j.1432-1033.1997.t01-1-00670.x;
RA Sauer K., Harms U., Thauer R.K.;
RT "Methanol:coenzyme M methyltransferase from Methanosarcina barkeri.
RT Purification, properties and encoding genes of the corrinoid protein MT1.";
RL Eur. J. Biochem. 243:670-677(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [3]
RP IDENTIFICATION.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=6438059; DOI=10.1128/jb.160.2.629-635.1984;
RA van der Meijden P., te Brommelstroet B.W., Poirot C.M., van der Drift C.,
RA Vogels G.D.;
RT "Purification and properties of methanol:5-hydroxybenzimidazolylcobamide
RT methyltransferase from Methanosarcina barkeri.";
RL J. Bacteriol. 160:629-635(1984).
RN [4]
RP IDENTIFICATION.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=9363780; DOI=10.1111/j.1432-1033.1997.t01-1-00280.x;
RA Sauer K., Thauer R.K.;
RT "Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Zinc
RT dependence and thermodynamics of the methanol:cob(I)alamin
RT methyltransferase reaction.";
RL Eur. J. Biochem. 249:280-285(1997).
RN [5]
RP COBALT-BINDING, AND MUTAGENESIS OF HIS-129; HIS-136 AND 256-HIS--HIS-258.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=9654068; DOI=10.1046/j.1432-1327.1998.2530698.x;
RA Sauer K., Thauer R.K.;
RT "Methanol:coenzyme M methyltransferase from Methanosarcina barkeri
RT -- identification of the active-site histidine in the corrinoid-harboring
RT subunit MtaC by site-directed mutagenesis.";
RL Eur. J. Biochem. 253:698-705(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MTAB, INTERACTION
RP WITH MTAB, AND SUBUNIT.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=17142327; DOI=10.1073/pnas.0603650103;
RA Hagemeier C.H., Krer M., Thauer R.K., Warkentin E., Ermler U.;
RT "Insight into the mechanism of biological methanol activation based on the
RT crystal structure of the methanol-cobalamin methyltransferase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18917-18922(2006).
CC -!- FUNCTION: Harbors a corrinoid prosthetic group and acts as a methyl
CC group carrier in methanogenesis in the methanol pathway. The methyl
CC group of methanol is first transferred to the corrinoid prosthetic
CC group of MtaC in the cob(I)amide oxidation state. This reaction is
CC mediated by MtaB. The methyl group from MtaC is then transferred to
CC coenzyme M by MtaA. {ECO:0000269|PubMed:9057830}.
CC -!- SUBUNIT: Heterotetramer, composed of 2 MtaB and 2 MtaC subunits.
CC {ECO:0000269|PubMed:17142327}.
CC -!- INTERACTION:
CC Q46EH4; Q46EH3: mtaB; NbExp=2; IntAct=EBI-9021153, EBI-9021160;
CC -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC {ECO:0000305}.
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DR EMBL; Y08310; CAA69619.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ69718.1; -; Genomic_DNA.
DR RefSeq; WP_011305768.1; NC_007355.1.
DR PDB; 2I2X; X-ray; 2.50 A; B/D/F/H/J/L/N/P=1-258.
DR PDBsum; 2I2X; -.
DR AlphaFoldDB; Q46EH4; -.
DR SMR; Q46EH4; -.
DR DIP; DIP-61321N; -.
DR IntAct; Q46EH4; 1.
DR STRING; 269797.Mbar_A0740; -.
DR EnsemblBacteria; AAZ69718; AAZ69718; Mbar_A0740.
DR GeneID; 3624441; -.
DR KEGG; mba:Mbar_A0740; -.
DR eggNOG; arCOG02032; Archaea.
DR HOGENOM; CLU_082102_0_0_2; -.
DR OMA; GYCADAM; -.
DR OrthoDB; 54330at2157; -.
DR BioCyc; MetaCyc:MTACMBARK-MON; -.
DR BRENDA; 2.1.1.90; 3250.
DR EvolutionaryTrace; Q46EH4; -.
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:InterPro.
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.
FT CHAIN 1..258
FT /note="Methanol--corrinoid protein"
FT /id="PRO_0000418941"
FT DOMAIN 30..124
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT DOMAIN 123..248
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 136
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 MUTAGEN 129
FT /note="H->K: Does not affect cobalamin-binding."
FT /evidence="ECO:0000269|PubMed:9654068"
FT MUTAGEN 136
FT /note="H->G,K: Abolishes cobalamin-binding."
FT /evidence="ECO:0000269|PubMed:9654068"
FT MUTAGEN 256..258
FT /note="HKH->KKK: Does not affect cobalamin-binding."
FT /evidence="ECO:0000269|PubMed:9654068"
FT CONFLICT 53
FT /note="D -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:2I2X"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 95..113
FT /evidence="ECO:0007829|PDB:2I2X"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2I2X"
FT TURN 185..189
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:2I2X"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:2I2X"
SQ SEQUENCE 258 AA; 27857 MW; C6D446CD1762B0A0 CRC64;
MLDFTEASLK KVLTRYNVAL EKALTPEEAA EELYPKDELI YPIAKAIFEG EEDDVVEGLQ
AAIEAGKDPI DLIDDALMVG MGVVIRLYDE GVIFLPNVMM SADAMLEGIE YCKENSGATP
KTKGTVVCHV AEGDVHDIGK NIVTALLRAN GYNVVDLGRD VPAEEVLAAV QKEKPIMLTG
TALMTTTMYA FKEVNDMLLE NGIKIPFACG GGAVNQDFVS QFALGVYGEE AADAPKIADA
IIAGTTDVTE LREKFHKH
