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MCH_CERS4
ID   MCH_CERS4               Reviewed;         343 AA.
AC   Q3IZ78;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Mesaconyl-CoA hydratase;
DE            EC=4.2.1.148;
DE   AltName: Full=2-methylfumaryl-CoA hydratase;
DE   AltName: Full=Beta-methylmalyl-CoA dehydratase;
GN   Name=mch; ORFNames=RSP_0973;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RX   PubMed=16856937; DOI=10.1111/j.1365-2958.2006.05238.x;
RA   Alber B.E., Spanheimer R., Ebenau-Jehle C., Fuchs G.;
RT   "Study of an alternate glyoxylate cycle for acetate assimilation by
RT   Rhodobacter sphaeroides.";
RL   Mol. Microbiol. 61:297-309(2006).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
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).
CC   -!- FUNCTION: Involved in the ethylmalonyl-CoA pathway for acetate
CC       assimilation. Catalyzes the reversible hydration of mesaconyl-CoA (2-
CC       methylfumaryl-CoA) to yield beta-methylmalyl-CoA ((2R,3S)-beta-
CC       methylmalyl-CoA). {ECO:0000269|PubMed:16856937,
CC       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   -!- INDUCTION: Strongly up-regulated during growth on acetate as sole
CC       carbon source. {ECO:0000269|PubMed:16856937}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to grow on
CC       acetate as a sole carbon source. {ECO:0000269|PubMed:16856937}.
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DR   EMBL; CP000143; ABA80156.1; -; Genomic_DNA.
DR   RefSeq; WP_011338635.1; NZ_CP030271.1.
DR   RefSeq; YP_354057.1; NC_007493.2.
DR   AlphaFoldDB; Q3IZ78; -.
DR   SMR; Q3IZ78; -.
DR   STRING; 272943.RSP_0973; -.
DR   EnsemblBacteria; ABA80156; ABA80156; RSP_0973.
DR   KEGG; rsp:RSP_0973; -.
DR   PATRIC; fig|272943.9.peg.2945; -.
DR   eggNOG; COG2030; Bacteria.
DR   OMA; RLIYGGH; -.
DR   PhylomeDB; Q3IZ78; -.
DR   BioCyc; MetaCyc:MON-13587; -.
DR   Proteomes; UP000002703; Chromosome 1.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IDA:UniProtKB.
DR   GO; GO:0045733; P:acetate 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; 1.
DR   PIRSF; PIRSF021494; Rv0216_prd; 1.
DR   SUPFAM; SSF54637; SSF54637; 2.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..343
FT                   /note="Mesaconyl-CoA hydratase"
FT                   /id="PRO_0000429582"
FT   DOMAIN          47..116
FT                   /note="MaoC-like"
FT   BINDING         60..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         83..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  37152 MW;  9107F5E1C4E691B5 CRC64;
     MKTNAGRFFE DYRLGETIAH AVPRTVSGGE RALYHALYPA RHALSSSDEF ARACGLPAAP
     VDELMAFHLV FGKTVPDISL NAVANLGYAE GRWLKPVFPG DTLRAESTVI GLKENSNGAS
     GVVWVRTRGL NQQGEAVLSY VRWVMVRKRD TAAPAPAPTV PELAGSVAAS DLVIPEGLSF
     TDYDLTLAGE PHRWGDYAVG EKIDHVDGVT VEESEHMLAT RLWQNTAKVH FDATNRPDGR
     RLIYGGHVIS LARTLSFNGL ANAQMIVALN AGAHANPCFA GDTVRAWSEV LDKAETADPG
     VGALRLRLVA MKHGTEPFVT RSEDGKYLPG VLLDLDYWAL VPR
 
 
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