CARC_PECCC
ID CARC_PECCC Reviewed; 273 AA.
AC Q9XB59;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=(5R)-carbapenem-3-carboxylate synthase;
DE EC=1.14.20.3;
DE AltName: Full=Carbapenem synthase;
GN Name=carC;
OS Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS carotovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=555;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 39048 / GS101;
RX PubMed=9402024; DOI=10.1046/j.1365-2958.1997.6001974.x;
RA McGowan S.J., Sebaihia M., O'Leary S., Hardie K.R., Williams P.,
RA Stewart G.S., Bycroft B.W., Salmond G.P.;
RT "Analysis of the carbapenem gene cluster of Erwinia carotovora: definition
RT of the antibiotic biosynthetic genes and evidence for a novel beta-lactam
RT resistance mechanism.";
RL Mol. Microbiol. 26:545-556(1997).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12848554; DOI=10.1021/ja034248a;
RA Stapon A., Li R., Townsend C.A.;
RT "Carbapenem biosynthesis: confirmation of stereochemical assignments and
RT the role of CarC in the ring stereoinversion process from L-proline.";
RL J. Am. Chem. Soc. 125:8486-8493(2003).
RN [3]
RP FUNCTION, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=15174175; DOI=10.1002/cbic.200300908;
RA Sleeman M.C., Smith P., Kellam B., Chhabra S.R., Bycroft B.W.,
RA Schofield C.J.;
RT "Biosynthesis of carbapenem antibiotics: new carbapenam substrates for
RT carbapenem synthase (CarC).";
RL ChemBioChem 5:879-882(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON;
RP N-ACETYLPROLINE AND 2-OXOGLUTARATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT,
RP ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=12611886; DOI=10.1074/jbc.m213054200;
RA Clifton I.J., Doan L.X., Sleeman M.C., Topf M., Suzuki H., Wilmouth R.C.,
RA Schofield C.J.;
RT "Crystal structure of carbapenem synthase (CarC).";
RL J. Biol. Chem. 278:20843-20850(2003).
CC -!- FUNCTION: Catalyzes the Fe(2+) and alpha-ketoglutarate-dependent
CC conversion of (3S,5S)-carbapenam to (5R)-carbapenem, an essential step
CC in carbapenem antibiotic biosynthesis. {ECO:0000269|PubMed:12611886,
CC ECO:0000269|PubMed:12848554, ECO:0000269|PubMed:15174175,
CC ECO:0000269|PubMed:9402024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S,5S)-carbapenam-3-caboxylate + 2-oxoglutarate + O2 = (5R)-
CC carbapenem-3-carboxylate + CO2 + H2O + succinate;
CC Xref=Rhea:RHEA:36611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:73939, ChEBI:CHEBI:73943; EC=1.14.20.3;
CC Evidence={ECO:0000269|PubMed:12611886, ECO:0000269|PubMed:12848554,
CC ECO:0000269|PubMed:15174175};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:12611886, ECO:0000269|PubMed:15174175};
CC Note=Binds 1 Fe(2+) per subunit. {ECO:0000269|PubMed:12611886,
CC ECO:0000269|PubMed:15174175};
CC -!- ACTIVITY REGULATION: Inhibited by L-N-acetylproline and by D-N-
CC acetylproline. {ECO:0000269|PubMed:12611886}.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000269|PubMed:12611886}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9402024}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; U17224; AAD38231.1; -; Genomic_DNA.
DR RefSeq; WP_039277159.1; NZ_QHMC01000009.1.
DR PDB; 1NX4; X-ray; 2.40 A; A/B/C=1-273.
DR PDB; 1NX8; X-ray; 2.30 A; A/B/C=1-273.
DR PDB; 4OJ8; X-ray; 2.10 A; A/B/C=1-273.
DR PDBsum; 1NX4; -.
DR PDBsum; 1NX8; -.
DR PDBsum; 4OJ8; -.
DR AlphaFoldDB; Q9XB59; -.
DR SMR; Q9XB59; -.
DR DrugBank; DB03360; N-Acetylproline.
DR PRIDE; Q9XB59; -.
DR BioCyc; MetaCyc:MON-13573; -.
DR BRENDA; 1.14.20.3; 2140.
DR EvolutionaryTrace; Q9XB59; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Cytoplasm; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..273
FT /note="(5R)-carbapenem-3-carboxylate synthase"
FT /id="PRO_0000424199"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12611886"
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12611886"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12611886"
FT BINDING 253
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT BINDING 263
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT BINDING 267
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4OJ8"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:4OJ8"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:4OJ8"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:4OJ8"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:4OJ8"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:4OJ8"
SQ SEQUENCE 273 AA; 31611 MW; 86F1AED4B09E84E4 CRC64;
MSEIVKFNPV MASGFGAYID HRDFLEAKTE TIKNLLMRQG FVVVKNLDID SDTFRDIYSA
YGTIVEYADE KIGVGFGYRD TLKLEGEKGK IVTGRGQLPF HADGGLLLSQ VDQVFLYAAE
IKNVKFRGAT TVCDHALACQ EMPAHLLRVL EEETFEVRVL ERGYYVDVSP DGWFKVPVFT
DLGWVRKMLI YFPFDEGQPA SWEPRIVGFT DHETQAFFQE LGAFLKQPRY YYKHFWEDGD
LLIMDNRRVI HEREEFNDDD IVRRLYRGQT ADI
