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Protein

(5R)-carbapenem-3-carboxylate synthase

Gene

carC

Organism
Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the Fe2+ and alpha-ketoglutarate-dependent conversion of (3S,5S)-carbapenam to (5R)-carbapenem, an essential step in carbapenem antibiotic biosynthesis.4 Publications

Catalytic activityi

(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O.3 Publications

Cofactori

Fe2+2 PublicationsNote: Binds 1 Fe2+ per subunit.2 Publications

Enzyme regulationi

Inhibited by L-N-acetylproline and by D-N-acetylproline.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi101Iron; catalytic1 Publication1
Metal bindingi103Iron; catalytic1 Publication1
Binding sitei104Substrate; via amide nitrogenSequence analysis1
Binding sitei130Alpha-ketoglutarate1
Metal bindingi251Iron; catalytic1 Publication1
Binding sitei253Alpha-ketoglutarate1
Binding sitei263Alpha-ketoglutarate1
Binding sitei267Alpha-ketoglutarate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13573.
BRENDAi1.14.20.3. 2140.

Names & Taxonomyi

Protein namesi
Recommended name:
(5R)-carbapenem-3-carboxylate synthase (EC:1.14.20.3)
Alternative name(s):
Carbapenem synthase
Gene namesi
Name:carC
OrganismiPectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)
Taxonomic identifieri555 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaePectobacterium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004241991 – 273(5R)-carbapenem-3-carboxylate synthaseAdd BLAST273

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.1 Publication

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 19Combined sources4
Helixi21 – 26Combined sources6
Helixi29 – 39Combined sources11
Beta strandi41 – 44Combined sources4
Helixi51 – 59Combined sources9
Beta strandi62 – 64Combined sources3
Helixi69 – 71Combined sources3
Beta strandi81 – 84Combined sources4
Beta strandi94 – 96Combined sources3
Beta strandi98 – 101Combined sources4
Helixi107 – 109Combined sources3
Beta strandi112 – 123Combined sources12
Beta strandi125 – 128Combined sources4
Beta strandi130 – 133Combined sources4
Helixi135 – 141Combined sources7
Helixi144 – 152Combined sources9
Beta strandi155 – 159Combined sources5
Helixi162 – 165Combined sources4
Turni166 – 168Combined sources3
Beta strandi178 – 181Combined sources4
Beta strandi186 – 188Combined sources3
Beta strandi201 – 206Combined sources6
Helixi211 – 225Combined sources15
Turni228 – 230Combined sources3
Beta strandi231 – 234Combined sources4
Beta strandi241 – 245Combined sources5
Turni246 – 248Combined sources3
Beta strandi250 – 253Combined sources4
Beta strandi262 – 271Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NX4X-ray2.40A/B/C1-273[»]
1NX8X-ray2.30A/B/C1-273[»]
4OJ8X-ray2.10A/B/C1-273[»]
ProteinModelPortaliQ9XB59.
SMRiQ9XB59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XB59.

Family & Domainsi

Sequence similaritiesi

Belongs to the TfdA dioxygenase family.Curated

Family and domain databases

InterProiIPR003819. TauD/TfdA-like.
[Graphical view]
PfamiPF02668. TauD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9XB59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEIVKFNPV MASGFGAYID HRDFLEAKTE TIKNLLMRQG FVVVKNLDID
60 70 80 90 100
SDTFRDIYSA YGTIVEYADE KIGVGFGYRD TLKLEGEKGK IVTGRGQLPF
110 120 130 140 150
HADGGLLLSQ VDQVFLYAAE IKNVKFRGAT TVCDHALACQ EMPAHLLRVL
160 170 180 190 200
EEETFEVRVL ERGYYVDVSP DGWFKVPVFT DLGWVRKMLI YFPFDEGQPA
210 220 230 240 250
SWEPRIVGFT DHETQAFFQE LGAFLKQPRY YYKHFWEDGD LLIMDNRRVI
260 270
HEREEFNDDD IVRRLYRGQT ADI
Length:273
Mass (Da):31,611
Last modified:November 1, 1999 - v1
Checksum:i86F1AED4B09E84E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17224 Genomic DNA. Translation: AAD38231.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17224 Genomic DNA. Translation: AAD38231.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NX4X-ray2.40A/B/C1-273[»]
1NX8X-ray2.30A/B/C1-273[»]
4OJ8X-ray2.10A/B/C1-273[»]
ProteinModelPortaliQ9XB59.
SMRiQ9XB59.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13573.
BRENDAi1.14.20.3. 2140.

Miscellaneous databases

EvolutionaryTraceiQ9XB59.

Family and domain databases

InterProiIPR003819. TauD/TfdA-like.
[Graphical view]
PfamiPF02668. TauD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARC_PECCC
AccessioniPrimary (citable) accession number: Q9XB59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.