MTAB_METBF
ID MTAB_METBF Reviewed; 461 AA.
AC Q46EH3; P94921;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Methanol--corrinoid protein co-methyltransferase;
DE EC=2.1.1.90;
DE AltName: Full=Methanol:corrinoid methyltransferase 1 subunit of 50 kDa;
DE Short=MT1 subunit 50 kDa;
GN Name=mtaB; OrderedLocusNames=Mbar_A0741;
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 2-24; 112-119;
RP 386-394; 427-438 AND 453-460, FUNCTION, AND CATALYTIC ACTIVITY.
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 FUNCTION, AND CATALYTIC ACTIVITY.
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 X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MTAC AND ZINC,
RP INTERACTION WITH MTAC, 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: Methyltransferase involved in methanogenesis in the methanol
CC pathway. Catalyzes the methylation of the MtaC-bound cob(I)amide.
CC {ECO:0000269|PubMed:9057830, ECO:0000269|PubMed:9363780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co(I)-[methanol-specific corrinoid protein] + H(+) + methanol
CC = H2O + methyl-Co(III)-[methanol-specific corrinoid protein];
CC Xref=Rhea:RHEA:45204, Rhea:RHEA-COMP:17570, Rhea:RHEA-COMP:17571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16379,
CC ChEBI:CHEBI:17790, ChEBI:CHEBI:60494; EC=2.1.1.90;
CC Evidence={ECO:0000269|PubMed:9057830, ECO:0000269|PubMed:9363780};
CC -!- SUBUNIT: Heterotetramer, composed of 2 MtaB and 2 MtaC subunits.
CC {ECO:0000269|PubMed:17142327}.
CC -!- INTERACTION:
CC Q46EH3; Q46EH4: mtaC; NbExp=2; IntAct=EBI-9021160, EBI-9021153;
CC -!- SIMILARITY: Belongs to the MtaB family. {ECO:0000305}.
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DR EMBL; Y08310; CAA69620.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ69719.1; -; Genomic_DNA.
DR RefSeq; WP_011305769.1; NC_007355.1.
DR PDB; 2I2X; X-ray; 2.50 A; A/C/E/G/I/K/M/O=1-461.
DR PDBsum; 2I2X; -.
DR AlphaFoldDB; Q46EH3; -.
DR SMR; Q46EH3; -.
DR DIP; DIP-61320N; -.
DR IntAct; Q46EH3; 1.
DR STRING; 269797.Mbar_A0741; -.
DR EnsemblBacteria; AAZ69719; AAZ69719; Mbar_A0741.
DR GeneID; 3624442; -.
DR KEGG; mba:Mbar_A0741; -.
DR eggNOG; arCOG03330; Archaea.
DR HOGENOM; CLU_588790_0_0_2; -.
DR OMA; CWSNESV; -.
DR OrthoDB; 11190at2157; -.
DR BioCyc; MetaCyc:MTABMBARK-MON; -.
DR BRENDA; 2.1.1.90; 3250.
DR EvolutionaryTrace; Q46EH3; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047152; F:methanol-5-hydroxybenzimidazolylcobamide Co-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR InterPro; IPR021079; MeOH-cob_MeTrfase_bsu.
DR Pfam; PF12176; MtaB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Methyltransferase;
KW Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9057830"
FT CHAIN 2..461
FT /note="Methanol--corrinoid protein co-methyltransferase"
FT /id="PRO_0000418930"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17142327"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17142327"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17142327"
FT CONFLICT 437
FT /note="D -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 55..76
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 95..116
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:2I2X"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 191..210
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2I2X"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2I2X"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 325..345
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 349..361
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 372..383
FT /evidence="ECO:0007829|PDB:2I2X"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 389..409
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 416..430
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 436..450
FT /evidence="ECO:0007829|PDB:2I2X"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:2I2X"
SQ SEQUENCE 461 AA; 50793 MW; 2ED12968E48D575B CRC64;
MAAKRYTSMA YANADEMTFG VSKYPVKAGL DLEIGAGYTI PEINYAPRPE AGASKEKLIK
EYERITTDVM ERMVQVGFPA IILETEHVQQ MSNNPSWGAE VAHAQKTIME KYHDEYGIKC
ALRHTIGDIR ENREFLQLRG DKYSVFLEAF EQCAENGADL LSVESMGGKE VFDYAVLRND
IPGLLYSIGC LGSIDMELIW TDISKIAKKT GTISAGDTDC AQANTAMFIG GGLLNKNLAH
TIAVIARAIS APRSLVAYEA GAVGPGKDCG YENIIVKAIT GMPMTMEGKT STCAHSDVMG
NLVMQCCDCW SNESVEYHGE FGGTTVQCWS ETLAYDCALM NTALETKNDK VLRDLMMLSD
RYRDPQAYML AYDNAYRVGQ SIVKDGDNIY LRAKNAAIEC CNIIEEGAAG KLELSRFETK
ALADAKAALE ALPDDMDKFM DDCLTKYKSE VKVFKPENYG F
