MUTB_PORGI
ID MUTB_PORGI Reviewed; 715 AA.
AC Q59677;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Methylmalonyl-CoA mutase large subunit;
DE EC=5.4.99.2;
DE AltName: Full=MCM-alpha;
GN Name=mutB; Synonyms=mcmB; OrderedLocusNames=PG_1657;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 53978 / W50;
RX PubMed=8566763; DOI=10.1016/0378-1119(95)00682-6;
RA Jackson C.A., Kirzbaum L., Dashper S., Reynolds E.C.;
RT "Cloning, expression and sequence analysis of the genes encoding the
RT heterodimeric methylmalonyl-CoA mutase of Porphyromonas gingivalis W50.";
RL Gene 167:127-132(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-
CC CoA during synthesis of propionate from tricarboxylic acid-cycle
CC intermediates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; L30136; AAB51084.1; -; Genomic_DNA.
DR EMBL; AE015924; AAQ66676.1; -; Genomic_DNA.
DR PIR; JC4560; JC4560.
DR RefSeq; WP_005875477.1; NC_002950.2.
DR AlphaFoldDB; Q59677; -.
DR SMR; Q59677; -.
DR STRING; 242619.PG_1657; -.
DR PRIDE; Q59677; -.
DR EnsemblBacteria; AAQ66676; AAQ66676; PG_1657.
DR KEGG; pgi:PG_1657; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_10; -.
DR OMA; PWGGSAY; -.
DR OrthoDB; 154460at2; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..715
FT /note="Methylmalonyl-CoA mutase large subunit"
FT /id="PRO_0000194272"
FT DOMAIN 587..715
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 70
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 73
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 77
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 80
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 82
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 84
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 109
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 112
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 134
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 190
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 192
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 201
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 202
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 202
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 239
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 278
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 280
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 328
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 365
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 368
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 599
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 600
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 601
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 602
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 645
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 647
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 676
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 699
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT SITE 84
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P11653"
SQ SEQUENCE 715 AA; 78703 MW; 766FDC92E13FBEB4 CRC64;
MKPNYKDIDI KSAGFVAKDA TRWAEEKGIV ADWRTPEQIM VKPLYTKDDL EGMEHLDYVS
GLPPFLRGPY SGMYPMRPWT IRQYAGFSTA EESNAFYRRN LASGQKGLSV AFDLATHRGY
DADHSRVVGD VGKAGVSICS LEDMKVLFDG IPLSKMSVSM TMNGAVLPIL AFYINAGLEQ
GAKLEEMAGT IQNDILKEFM VRNTYIYPPE FSMRIIADIF EYTSQNMPKF NSISISGYHM
QEAGATADIE MAYTLADGMQ YLKAGIDAGI DVDAFAPRLS FFWAIGVNHF MEIAKMRAAR
LLWAKIVKSF GAKNPKSLAL RTHSQTSGWS LTEQDPFNNV GRTCIEAMAA ALGHTQSLHT
NALDEAIALP TDFSARIARN TQIYIQEETL VCKEIDPWGG SYYVESLTNE LVHKAWTLIK
EVQEMGGMAK AIETGLPKLR IEEAAARTQA RIDSHQQVIV GVNKYRLPKE DPIDILEIDN
TAVRKQQIER LNDLRSHRDE KAVQEALEAI TKCVETKEGN LLDLAVKAAG LRASLGEISD
ACEKVVGRYK AVIRTISGVY SSESGEDKDF AHAKELAEKF AKKEGRQPRI MIAKMGQDGH
DRGAKVVATG YADCGFDVDM GPLFQTPEEA ARQAVENDVH VMGVSSLAAG HKTLIPQVIA
ELEKLGRPDI LVTAGGVIPA QDYDFLYQAG VAAIFGPGTP VAYSAAKVLE ILLEE
