ACSE_MOOTH
ID ACSE_MOOTH Reviewed; 262 AA.
AC Q46389;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase;
DE EC=2.1.1.258;
DE AltName: Full=5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase;
DE Short=MeTr;
GN Name=acsE;
OS Moorella thermoacetica (Clostridium thermoaceticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=1525;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 35608 / DSM 521 / JCM 9319;
RX PubMed=7928975; DOI=10.1128/jb.176.19.6127-6130.1994;
RA Roberts D.L., Zhao S., Doukov T., Ragsdale S.W.;
RT "The reductive acetyl coenzyme A pathway: sequence and heterologous
RT expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein
RT methyltransferase from Clostridium thermoaceticum.";
RL J. Bacteriol. 176:6127-6130(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RX PubMed=10997901; DOI=10.1016/s0969-2126(00)00172-6;
RA Doukov T., Seravalli J., Stezowski J.J., Ragsdale S.W.;
RT "Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent
RT methyltransferase.";
RL Structure 8:817-830(2000).
RN [3] {ECO:0007744|PDB:2E7F, ECO:0007744|PDB:2OGY}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH
RP METHYLTETRAHYDROFOLATE AND CALCIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND MUTAGENESIS OF ASN-199.
RX PubMed=17172470; DOI=10.1074/jbc.m609828200;
RA Doukov T.I., Hemmi H., Drennan C.L., Ragsdale S.W.;
RT "Structural and kinetic evidence for an extended hydrogen-bonding network
RT in catalysis of methyl group transfer. Role of an active site asparagine
RT residue in activation of methyl transfer by methyltransferases.";
RL J. Biol. Chem. 282:6609-6618(2007).
RN [4] {ECO:0007744|PDB:4DJD, ECO:0007744|PDB:4DJE, ECO:0007744|PDB:4DJF}
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH ACSC; ACSD;
RP METHYLTETRAHYDROFOLATE; COBALAMIN AND CALCIUM, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=22419154; DOI=10.1038/nature10916;
RA Kung Y., Ando N., Doukov T.I., Blasiak L.C., Bender G., Seravalli J.,
RA Ragsdale S.W., Drennan C.L.;
RT "Visualizing molecular juggling within a B12-dependent methyltransferase
RT complex.";
RL Nature 484:265-269(2012).
CC -!- FUNCTION: Methyltransferase that mediates the transfer of a N5-methyl
CC group of (6S)-methyltetrahydrofolate to the 5-
CC methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein
CC (AcsC/AcsD) in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl
CC pathway) of carbon monoxide and carbon dioxide fixation.
CC {ECO:0000269|PubMed:17172470, ECO:0000269|PubMed:22419154,
CC ECO:0000269|PubMed:7928975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + methyl-Co(III)-[corrinoid Fe-S
CC protein] = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + Co(I)-[corrinoid
CC Fe-S protein] + H(+); Xref=Rhea:RHEA:45200, Rhea:RHEA-COMP:11110,
CC Rhea:RHEA-COMP:11111, ChEBI:CHEBI:15378, ChEBI:CHEBI:18608,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:85033, ChEBI:CHEBI:85035;
CC EC=2.1.1.258; Evidence={ECO:0000269|PubMed:17172470,
CC ECO:0000269|PubMed:22419154, ECO:0000269|PubMed:7928975};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17172470, ECO:0000269|PubMed:22419154};
CC -!- SUBUNIT: Heterohexamer composed of 2 subunits of AcsC, 2 subunits of
CC AcsD and 2 subunits of AcsE. {ECO:0000269|PubMed:17172470,
CC ECO:0000269|PubMed:22419154}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L34780; AAA53548.2; -; Genomic_DNA.
DR PIR; I40795; I40795.
DR RefSeq; WP_011392711.1; NZ_VCDY01000001.1.
DR PDB; 1F6Y; X-ray; 2.20 A; A/B=1-262.
DR PDB; 2E7F; X-ray; 2.20 A; A/B=1-262.
DR PDB; 2OGY; X-ray; 2.30 A; A/B=1-262.
DR PDB; 4DJD; X-ray; 2.38 A; A/B=1-262.
DR PDB; 4DJE; X-ray; 3.50 A; A/B=1-262.
DR PDB; 4DJF; X-ray; 3.03 A; A/B=1-262.
DR PDBsum; 1F6Y; -.
DR PDBsum; 2E7F; -.
DR PDBsum; 2OGY; -.
DR PDBsum; 4DJD; -.
DR PDBsum; 4DJE; -.
DR PDBsum; 4DJF; -.
DR AlphaFoldDB; Q46389; -.
DR SMR; Q46389; -.
DR DIP; DIP-59668N; -.
DR IntAct; Q46389; 1.
DR GeneID; 61289915; -.
DR OMA; RINGMFK; -.
DR OrthoDB; 981229at2; -.
DR BioCyc; MetaCyc:METHCOCLTH-MON; -.
DR BRENDA; 2.1.1.258; 1528.
DR EvolutionaryTrace; Q46389; -.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0102036; F:methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.20; -; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR000489; Pterin-binding_dom.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbon dioxide fixation; Cobalamin; Cobalt;
KW Metal-binding; Methyltransferase; Transferase.
FT CHAIN 1..262
FT /note="5-methyltetrahydrofolate:corrinoid/iron-sulfur
FT protein co-methyltransferase"
FT /id="PRO_0000422560"
FT DOMAIN 1..246
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT BINDING 96
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154, ECO:0007744|PDB:4DJE,
FT ECO:0007744|PDB:4DJF"
FT BINDING 160
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154, ECO:0007744|PDB:4DJE,
FT ECO:0007744|PDB:4DJF"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154"
FT BINDING 199
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154, ECO:0007744|PDB:4DJE,
FT ECO:0007744|PDB:4DJF"
FT BINDING 202..203
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000305|PubMed:22419154,
FT ECO:0007744|PDB:4DJF"
FT BINDING 202
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154, ECO:0007744|PDB:4DJF"
FT BINDING 207
FT /ligand="(6S)-5-methyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:18608"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154, ECO:0007744|PDB:4DJE,
FT ECO:0007744|PDB:4DJF"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17172470,
FT ECO:0000269|PubMed:22419154"
FT SITE 199
FT /note="Transition state stabilizer"
FT MUTAGEN 199
FT /note="N->A: 20-fold decreased affinity for
FT methyltetrahydrofolate and nearly abolished catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:17172470"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:1F6Y"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:1F6Y"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1F6Y"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:1F6Y"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 133..150
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1F6Y"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1F6Y"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:1F6Y"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:1F6Y"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:1F6Y"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:1F6Y"
SQ SEQUENCE 262 AA; 28609 MW; 62466A25D42496A1 CRC64;
MLIIGERING MFGDIKRAIQ ERDPAPVQEW ARRQEEGGAR ALDLNVGPAV QDKVSAMEWL
VEVTQEVSNL TLCLDSTNIK AIEAGLKKCK NRAMINSTNA EREKVEKLFP LAVEHGAALI
GLTMNKTGIP KDSDTRLAFA MELVAAADEF GLPMEDLYID PLILPANVAQ DHAPEVLKTL
QQIKMLADPA PKTVLGLSNV SQNCQNRPLI NRTFLAMAMA CGLDAAIADA CDEALIETAA
TAEILLNQTV YCDSFVKMFK TR
