MCH_CHLAA
ID MCH_CHLAA Reviewed; 352 AA.
AC A9WC34;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Beta-methylmalyl-CoA dehydratase;
DE EC=4.2.1.148;
DE AltName: Full=2-methylfumaryl-CoA hydratase;
DE AltName: Full=Mesaconyl-CoA hydratase;
GN Name=mch; OrderedLocusNames=Caur_0173;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP SUBUNIT.
RC STRAIN=DSM 636 / Ok-70-fl;
RX PubMed=18065535; DOI=10.1128/jb.01621-07;
RA Zarzycki J., Schlichting A., Strychalsky N., Muller M., Alber B.E.,
RA Fuchs G.;
RT "Mesaconyl-coenzyme A hydratase, a new enzyme of two central carbon
RT metabolic pathways in bacteria.";
RL J. Bacteriol. 190:1366-1374(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RA Malashkevich V.N., Bhosle R., Toro R., Hillerich B., Gizzi A., Garforth S.,
RA Kar A., Chan M.K., Lafluer J., Patel H., Matikainen B., Chamala S., Lim S.,
RA Celikgil A., Villegas G., Evans B., Zenchek W., Love J., Fiser A.,
RA Khafizov K., Seidel R., Bonanno J.B., Almo S.C.;
RT "Crystal structure of putative MaoC domain protein dehydratase from
RT Chloroflexus aurantiacus J-10-fl.";
RL Submitted (MAR-2012) to the PDB data bank.
CC -!- FUNCTION: Involved in the glyoxylate assimilation cycle used to
CC regenerate acetyl-CoA and produce pyruvate as universal precursor for
CC biosynthesis. Catalyzes the reversible dehydration of beta-methylmalyl-
CC CoA ((2R,3S)-beta-methylmalyl-CoA) to yield mesaconyl-CoA (2-
CC methylfumaryl-CoA). {ECO:0000269|PubMed:18065535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-beta-methylmalyl-CoA = 2-methylfumaryl-CoA + H2O;
CC Xref=Rhea:RHEA:38263, ChEBI:CHEBI:15377, ChEBI:CHEBI:75634,
CC ChEBI:CHEBI:75635; EC=4.2.1.148;
CC Evidence={ECO:0000269|PubMed:18065535};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18065535};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18065535, ECO:0000269|Ref.3}.
CC -!- INDUCTION: Under autotrophic growth conditions.
CC {ECO:0000269|PubMed:18065535}.
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DR EMBL; CP000909; ABY33427.1; -; Genomic_DNA.
DR RefSeq; WP_012256083.1; NC_010175.1.
DR RefSeq; YP_001633816.1; NC_010175.1.
DR PDB; 4E3E; X-ray; 1.90 A; A/B=1-352.
DR PDBsum; 4E3E; -.
DR AlphaFoldDB; A9WC34; -.
DR SMR; A9WC34; -.
DR STRING; 324602.Caur_0173; -.
DR EnsemblBacteria; ABY33427; ABY33427; Caur_0173.
DR KEGG; cau:Caur_0173; -.
DR PATRIC; fig|324602.8.peg.200; -.
DR eggNOG; COG2030; Bacteria.
DR HOGENOM; CLU_067804_0_0_0; -.
DR InParanoid; A9WC34; -.
DR OMA; RLIYGGH; -.
DR BioCyc; MetaCyc:MON-17292; -.
DR BRENDA; 4.2.1.148; 1352.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0019171; F:3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IBA:GO_Central.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IDA:UniProtKB.
DR GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009436; P:glyoxylate catabolic process; IDA:UniProtKB.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR016790; Thiol_ester_hydratase_Rv0216.
DR Pfam; PF01575; MaoC_dehydratas; 2.
DR PIRSF; PIRSF021494; Rv0216_prd; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Carbon dioxide fixation; Lyase; Reference proteome.
FT CHAIN 1..352
FT /note="Beta-methylmalyl-CoA dehydratase"
FT /id="PRO_0000429581"
FT DOMAIN 16..129
FT /note="MaoC-like"
FT BINDING 62..65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96..98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:4E3E"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 104..116
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 120..132
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 138..149
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4E3E"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 288..300
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 305..319
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:4E3E"
FT STRAND 338..349
FT /evidence="ECO:0007829|PDB:4E3E"
SQ SEQUENCE 352 AA; 38704 MW; 9028FEDE99F5288F CRC64;
MSAKTNPGNF FEDFRLGQTI VHATPRTITE GDVALYTSLY GSRFALTSST PFAQSLGLER
APIDSLLVFH IVFGKTVPDI SLNAIANLGY AGGRFGAVVY PGDTLSTTSK VIGLRQNKDG
KTGVVYVHSV GVNQWDEVVL EYIRWVMVRK RDPNAPAPET VVPDLPDSVP VTDLTVPYTV
SAANYNLAHA GSNYLWDDYE VGEKIDHVDG VTIEEAEHMQ ATRLYQNTAR VHFNLHVERE
GRFGRRIVYG GHIISLARSL SFNGLANALS IAAINSGRHT NPSFAGDTIY AWSEILAKMA
IPGRTDIGAL RVRTVATKDR PCHDFPYRDA EGNYDPAVVL DFDYTVLMPR RG
