ID 5S_PROFR Reviewed; 505 AA. AC Q70AC7; Q05618; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 13-SEP-2023, entry version 76. DE RecName: Full=Methylmalonyl-CoA carboxyltransferase 5S subunit; DE EC=2.1.3.1; DE AltName: Full=Transcarboxylase 5S subunit; OS Propionibacterium freudenreichii subsp. shermanii. OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1752; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-22; 67-76; RP 88-92; 111-124; 134-147; 305-316; 325-337; 371-393; 397-410 AND 431-456. RC STRAIN=St33; RX PubMed=8365490; DOI=10.1016/0014-5793(93)80271-u; RA Thornton C.G., Kumar G.K., Shenoy B.C., Haase F.C., Phillips N.F.B., RA Park V.M., Magner W.J., Hejlik D.P., Wood H.G., Samols D.; RT "Primary structure of the 5 S subunit of transcarboxylase as deduced from RT the genomic DNA sequence."; RL FEBS Lett. 330:191-196(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13673 / NCIMB 10585 / NRRL B-4327 / VPI 409 / 33; RX PubMed=14993680; DOI=10.1107/s0907444903028294; RA Hall P.R., Zheng R., Pusztai-Carey M., van den Akker F., Carey P.R., RA Yee V.C.; RT "Expression and crystallization of several forms of the Propionibacterium RT shermanii transcarboxylase 5S subunit."; RL Acta Crystallogr. D 60:521-523(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; PRODUCT RP AND COBALT IONS, SUBUNIT, CARBOXYLATION AT LYS-184, AND MUTAGENESIS OF RP ALA-59; LYS-184 AND MET-186. RX PubMed=15329673; DOI=10.1038/sj.emboj.7600373; RA Hall P.R., Zheng R., Antony L., Pusztai-Carey M., Carey P.R., Yee V.C.; RT "Transcarboxylase 5S structures: assembly and catalytic mechanism of a RT multienzyme complex subunit."; RL EMBO J. 23:3621-3631(2004). CC -!- FUNCTION: The 5S subunit specifically catalyzes the transfer of the CC carboxyl group from biotin of the 1.3S subunit to pyruvate to form CC oxaloacetate and 1.3S biotin. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-methylmalonyl-CoA + pyruvate = oxaloacetate + propanoyl- CC CoA; Xref=Rhea:RHEA:20764, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57392; EC=2.1.3.1; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Note=Binds 1 Co(2+) ion per subunit.; CC -!- SUBUNIT: Homodimer. Transcarboxylase is composed of three subunits: CC 1.3S, 5S, and 12S. The core of the enzyme is composed of six 12S CC subunits. On each side of the core there are three pairs of 5S CC subunits. Each 5S dimer is attached to the core by two 1.3S subunits. CC Thus the total number of chains is 30 (6 + 12 + 12). CC {ECO:0000269|PubMed:15329673}. CC -!- PTM: Lys-184 is carboxylated in the free enzyme and helps to coordinate CC the cobalt ion. Lys-184 is partially carboxylated in the complex with CC pyruvate, but is not carboxylated in the oxaloacetate-bound form. CC {ECO:0000269|PubMed:15329673}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA03174.1; Type=Frameshift; Evidence={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; L06488; AAA03174.1; ALT_FRAME; Unassigned_DNA. DR EMBL; AJ606310; CAE54442.1; -; Genomic_DNA. DR PIR; S36808; S36808. DR PDB; 1RQB; X-ray; 1.90 A; A=2-505. DR PDB; 1RQE; X-ray; 2.50 A; A=2-505. DR PDB; 1RQH; X-ray; 2.00 A; A=2-505. DR PDB; 1RR2; X-ray; 2.00 A; A=2-505. DR PDB; 1S3H; X-ray; 2.50 A; A=2-505. DR PDB; 1U5J; X-ray; 2.80 A; A=2-505. DR PDBsum; 1RQB; -. DR PDBsum; 1RQE; -. DR PDBsum; 1RQH; -. DR PDBsum; 1RR2; -. DR PDBsum; 1S3H; -. DR PDBsum; 1U5J; -. DR AlphaFoldDB; Q70AC7; -. DR SMR; Q70AC7; -. DR DrugBank; DB04553; 2-Oxobutanoic Acid. DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid. DR DrugBank; DB02637; Oxaloacetate Ion. DR BioCyc; MetaCyc:MONOMER-12430; -. DR BRENDA; 2.1.3.1; 5032. DR EvolutionaryTrace; Q70AC7; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047154; F:methylmalonyl-CoA carboxytransferase activity; IEA:UniProtKB-EC. DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003379; Carboxylase_cons_dom. DR InterPro; IPR000891; PYR_CT. DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1. DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF02436; PYC_OADA; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR SUPFAM; SSF89000; post-HMGL domain-like; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalt; Direct protein sequencing; Metal-binding; KW Transferase. FT CHAIN 1..505 FT /note="Methylmalonyl-CoA carboxyltransferase 5S subunit" FT /id="PRO_0000146816" FT DOMAIN 14..276 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151" FT BINDING 22..26 FT /ligand="substrate" FT BINDING 23 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT BINDING 59 FT /ligand="substrate" FT BINDING 184 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT BINDING 184 FT /ligand="substrate" FT BINDING 215 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT BINDING 217 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT MOD_RES 184 FT /note="N6-carboxylysine; partial" FT /evidence="ECO:0000269|PubMed:15329673" FT MUTAGEN 59 FT /note="A->T: Decreases activity by 96%." FT /evidence="ECO:0000269|PubMed:15329673" FT MUTAGEN 184 FT /note="K->A,E: Loss of activity." FT /evidence="ECO:0000269|PubMed:15329673" FT MUTAGEN 186 FT /note="M->I: Decreases activity by 98%." FT /evidence="ECO:0000269|PubMed:15329673" FT CONFLICT 341 FT /note="A -> AG (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT CONFLICT 386 FT /note="S -> T (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT CONFLICT 390 FT /note="R -> RDPKWSVGEEHRRAITQRPADH (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT CONFLICT 421 FT /note="K -> E (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT CONFLICT 429 FT /note="L -> P (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT CONFLICT 455 FT /note="H -> S (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT CONFLICT 461 FT /note="H -> Q (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT CONFLICT 481 FT /note="L -> V (in Ref. 1; AAA03174)" FT /evidence="ECO:0000305" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 15..18 FT /evidence="ECO:0007829|PDB:1RQB" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 23..28 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 60..66 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 72..82 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 105..117 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 133..144 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 163..175 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 179..185 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 192..206 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 212..217 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:1U5J" FT HELIX 223..232 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 254..260 FT /evidence="ECO:0007829|PDB:1RQB" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:1RQB" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 272..285 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 286..292 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 302..305 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 309..320 FT /evidence="ECO:0007829|PDB:1RQB" FT TURN 325..327 FT /evidence="ECO:0007829|PDB:1U5J" FT HELIX 328..341 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 351..365 FT /evidence="ECO:0007829|PDB:1RQB" FT TURN 367..369 FT /evidence="ECO:0007829|PDB:1S3H" FT HELIX 373..379 FT /evidence="ECO:0007829|PDB:1RQB" FT TURN 380..383 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 392..402 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 411..414 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 419..426 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 436..444 FT /evidence="ECO:0007829|PDB:1RQB" FT TURN 446..448 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 449..455 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 456..458 FT /evidence="ECO:0007829|PDB:1RQB" FT HELIX 467..473 FT /evidence="ECO:0007829|PDB:1RQB" SQ SEQUENCE 505 AA; 55649 MW; 6DF657E231609064 CRC64; MSPREIEVSE PREVGITELV LRDAHQSLMA TRMAMEDMVG ACADIDAAGY WSVECWGGAT YDSCIRFLNE DPWERLRTFR KLMPNSRLQM LLRGQNLLGY RHYNDEVVDR FVDKSAENGM DVFRVFDAMN DPRNMAHAMA AVKKAGKHAQ GTICYTISPV HTVEGYVKLA GQLLDMGADS IALKDMAALL KPQPAYDIIK AIKDTYGQKT QINLHCHSTT GVTEVSLMKA IEAGVDVVDT AISSMSLGPG HNPTESVAEM LEGTGYTTNL DYDRLHKIRD HFKAIRPKYK KFESKTLVDT SIFKSQIPGG MLSNMESQLR AQGAEDKMDE VMAEVPRVRK AAGFPPLVTP SSQIVGTQAV FNVMMGEYKR MTGEFADIML GYYGASPADR DPKVVKLAEE QSGKKPITQR PADLLPPEWE KQSKEAATLK GFNGTDEDVL TYALFPQVAP VFFEHRAEGP HSVALTDAQL KAEAEGDEKS LAVAGPVTYN VNVGGTVREV TVQQA //