5S_PROFR
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 03-AUG-2022, entry version 71.
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; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC 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};
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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 PRIDE; Q70AC7; -.
DR BioCyc; MetaCyc:MON-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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 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
