ID   U2JSA4_PORGN            Unreviewed;       715 AA.
AC   U2JSA4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   ORFNames=HMPREF1989_02085 {ECO:0000313|EMBL:ERJ82912.1};
OS   Porphyromonas gingivalis F0566.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1321822 {ECO:0000313|EMBL:ERJ82912.1, ECO:0000313|Proteomes:UP000016609};
RN   [1] {ECO:0000313|EMBL:ERJ82912.1, ECO:0000313|Proteomes:UP000016609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0566 {ECO:0000313|EMBL:ERJ82912.1,
RC   ECO:0000313|Proteomes:UP000016609};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000256|ARBA:ARBA00008465}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERJ82912.1}.
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DR   EMBL; AWVD01000198; ERJ82912.1; -; Genomic_DNA.
DR   RefSeq; WP_005875477.1; NZ_KI259995.1.
DR   AlphaFoldDB; U2JSA4; -.
DR   SMR; U2JSA4; -.
DR   PATRIC; fig|1321822.3.peg.1759; -.
DR   HOGENOM; CLU_009523_3_1_10; -.
DR   Proteomes; UP000016609; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
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   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR   PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          587..715
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
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
//