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Protein

Beta-lactamase

Gene

ampC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801Acyl-ester intermediatePROSITE-ProRule annotation1 Publication
Active sitei166 – 1661Proton acceptor

GO - Molecular functioni

  • beta-lactamase activity Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

BioCyciEcoCyc:EG10040-MONOMER.
ECOL316407:JW4111-MONOMER.
MetaCyc:EG10040-MONOMER.
BRENDAi3.5.2.6. 2026.
SABIO-RKP00811.

Protein family/group databases

MEROPSiS12.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase (EC:3.5.2.6)
Alternative name(s):
Cephalosporinase
Gene namesi
Name:ampC
Synonyms:ampA
Ordered Locus Names:b4150, JW4111
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10040. ampC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801S → D, E or G: Loss of activity. 1 Publication
Mutagenesisi83 – 831K → Q or T: Lowers activity more than 1000-fold and increases protein stability. 1 Publication
Mutagenesisi166 – 1661Y → E: Lowers activity more than 1000-fold. 1 Publication
Mutagenesisi168 – 1681N → D or H: Lowers activity more than 1000-fold. 1 Publication
Mutagenesisi331 – 3311K → A: Lowers activity more than 1000-fold. 1 Publication

Chemistry

DrugBankiDB00456. Cefalotin.
DB01147. Cloxacillin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 377358Beta-lactamasePRO_0000016958Add
BLAST

2D gel databases

SWISS-2DPAGEP00811.

Expressioni

Gene expression databases

GenevestigatoriP00811.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP00811. 1 interaction.
STRINGi511145.b4150.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3918Combined sources
Beta strandi42 – 509Combined sources
Beta strandi53 – 6311Combined sources
Turni64 – 674Combined sources
Beta strandi75 – 773Combined sources
Helixi79 – 813Combined sources
Helixi82 – 9514Combined sources
Helixi105 – 1084Combined sources
Helixi115 – 1173Combined sources
Helixi122 – 1265Combined sources
Helixi144 – 15310Combined sources
Beta strandi162 – 1643Combined sources
Helixi168 – 17811Combined sources
Turni179 – 1835Combined sources
Helixi186 – 1938Combined sources
Turni194 – 1996Combined sources
Beta strandi204 – 2063Combined sources
Helixi209 – 2146Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2253Combined sources
Turni229 – 2313Combined sources
Helixi233 – 2364Combined sources
Beta strandi240 – 2423Combined sources
Helixi243 – 25412Combined sources
Helixi256 – 2583Combined sources
Helixi262 – 27110Combined sources
Beta strandi273 – 2786Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi288 – 2936Combined sources
Helixi296 – 3016Combined sources
Beta strandi303 – 3053Combined sources
Beta strandi306 – 3083Combined sources
Beta strandi310 – 3134Combined sources
Beta strandi315 – 3217Combined sources
Beta strandi325 – 33511Combined sources
Beta strandi338 – 3458Combined sources
Helixi346 – 3483Combined sources
Beta strandi350 – 3589Combined sources
Helixi362 – 37615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3BX-ray2.25A/B20-377[»]
1FCMX-ray2.46A/B20-377[»]
1FCNX-ray2.35A/B20-377[»]
1FCOX-ray2.20A/B20-377[»]
1FSWX-ray1.90A/B20-376[»]
1FSYX-ray1.75A/B20-376[»]
1GA9X-ray2.10A/B20-377[»]
1I5QX-ray1.83A/B20-377[»]
1IELX-ray2.00A/B20-377[»]
1IEMX-ray2.30A/B20-377[»]
1KDSX-ray2.15A/B20-377[»]
1KDWX-ray2.28A/B20-377[»]
1KE0X-ray2.30A/B20-377[»]
1KE3X-ray2.15A/B20-377[»]
1KE4X-ray1.72A/B20-377[»]
1KVLX-ray1.53A/B20-377[»]
1KVMX-ray2.06A/B20-377[»]
1L0DX-ray1.53A/B20-377[»]
1L0EX-ray1.90A/B20-377[»]
1L0FX-ray1.66A/B20-377[»]
1L0GX-ray1.50A/B20-377[»]
1L2SX-ray1.94A/B20-377[»]
1LL5X-ray1.80A/B20-377[»]
1LL9X-ray1.87A/B20-377[»]
1LLBX-ray1.72A/B20-377[»]
1MXOX-ray1.83A/B20-377[»]
1MY8X-ray1.72A/B20-377[»]
1O07X-ray1.71A/B20-377[»]
1PI4X-ray1.39A/B20-377[»]
1PI5X-ray1.49A/B20-377[»]
1XGIX-ray1.96A/B20-377[»]
1XGJX-ray1.97A/B20-377[»]
2BLSX-ray2.00A/B20-377[»]
2FFYX-ray1.07A/B20-377[»]
2HDQX-ray2.10A/B20-377[»]
2HDRX-ray2.20A/B20-377[»]
2HDSX-ray1.16A/B20-377[»]
2HDUX-ray1.49A/B20-377[»]
2I72X-ray2.20A/B20-377[»]
2P9VX-ray1.80A/B20-377[»]
2PU2X-ray1.86A/B20-377[»]
2PU4X-ray2.00A/B20-377[»]
2R9WX-ray1.80A/B20-377[»]
2R9XX-ray1.90A/B20-377[»]
2RCXX-ray2.00A/B20-377[»]
3BLSX-ray2.30A/B20-377[»]
3BM6X-ray2.10A/B20-377[»]
3FKVX-ray1.85A/B20-377[»]
3FKWX-ray1.50A/B20-377[»]
3GQZX-ray1.80A/B20-377[»]
3GR2X-ray1.80A/B20-377[»]
3GRJX-ray2.49A/B20-377[»]
3GSGX-ray2.10A/B20-377[»]
3GTCX-ray1.90A/B20-377[»]
3GV9X-ray1.80A/B20-377[»]
3GVBX-ray1.80A/B20-377[»]
3IWIX-ray1.64A/B20-377[»]
3IWOX-ray1.90A/B20-377[»]
3IWQX-ray1.84A/B20-377[»]
3IXBX-ray1.63A/B20-377[»]
3IXDX-ray2.64A/B20-377[»]
3IXGX-ray2.14A/B20-377[»]
3IXHX-ray2.30A/B20-377[»]
3O86X-ray1.60A/B20-377[»]
3O87X-ray1.78A/B20-377[»]
3O88X-ray1.64A/B20-377[»]
4E3IX-ray1.60A/B20-377[»]
4E3JX-ray1.80A/B20-377[»]
4E3KX-ray1.43A/B20-377[»]
4E3LX-ray1.43A/B20-377[»]
4E3MX-ray1.44A/B20-377[»]
4E3NX-ray1.49A/B20-377[»]
4E3OX-ray1.60A/B20-377[»]
4JXGX-ray1.65A/B20-377[»]
4JXSX-ray1.90A/B20-377[»]
4JXVX-ray1.76A/B20-377[»]
4JXWX-ray2.30A/B20-377[»]
4KENX-ray1.89B20-377[»]
4KG2X-ray1.89A/B20-377[»]
4KG5X-ray2.11A/B/C/D20-377[»]
4KG6X-ray1.75A/B/C/D20-377[»]
4KZ3X-ray1.67A/B20-377[»]
4KZ4X-ray1.42A/B20-377[»]
4KZ5X-ray1.35A/B20-377[»]
4KZ6X-ray1.68A/B20-377[»]
4KZ7X-ray1.43A/B20-377[»]
4KZ8X-ray2.28A/B20-377[»]
4KZ9X-ray1.72A/B20-377[»]
4KZAX-ray1.60A/B20-377[»]
4KZBX-ray1.37A/B20-377[»]
4LV0X-ray1.65A/B20-377[»]
4LV1X-ray1.74A/B20-377[»]
4LV2X-ray1.65A/B20-377[»]
4LV3X-ray1.42A/B20-377[»]
4OKPX-ray1.37A/B20-377[»]
4OLDX-ray1.48A/B20-377[»]
4OLGX-ray1.71A/B20-377[»]
ProteinModelPortaliP00811.
SMRiP00811. Positions 20-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00811.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 3333Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the class-C beta-lactamase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1680.
HOGENOMiHOG000267102.
InParanoidiP00811.
KOiK01467.
OMAiMQANINP.
OrthoDBiEOG60SCH1.
PhylomeDBiP00811.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY
60 70 80 90 100
QGKPYYFTWG YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK
110 120 130 140 150
LSDPTTKYWP ELTAKQWNGI TLLHLATYTA GGLPLQVPDE VKSSSDLLRF
160 170 180 190 200
YQNWQPAWAP GTQRLYANSS IGLFGALAVK PSGLSFEQAM QTRVFQPLKL
210 220 230 240 250
NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK STIEDMARWV
260 270 280 290 300
QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII
310 320 330 340 350
NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL
360 370
GIVMLANKNY PNPARVDAAW QILNALQ
Length:377
Mass (Da):41,556
Last modified:July 21, 1986 - v1
Checksum:i3C6FB4FE4EF96C9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23441.1.
U14003 Genomic DNA. Translation: AAA97049.1.
U00096 Genomic DNA. Translation: AAC77110.1.
AP009048 Genomic DNA. Translation: BAE78154.1.
V00277 Genomic DNA. Translation: CAA23537.1.
PIRiA01007. QKEC.
RefSeqiNP_418574.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC77110; AAC77110; b4150.
BAE78154; BAE78154; BAE78154.
GeneIDi948669.
KEGGiecj:Y75_p4039.
eco:b4150.
PATRICi32123873. VBIEscCol129921_4284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23441.1.
U14003 Genomic DNA. Translation: AAA97049.1.
U00096 Genomic DNA. Translation: AAC77110.1.
AP009048 Genomic DNA. Translation: BAE78154.1.
V00277 Genomic DNA. Translation: CAA23537.1.
PIRiA01007. QKEC.
RefSeqiNP_418574.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3BX-ray2.25A/B20-377[»]
1FCMX-ray2.46A/B20-377[»]
1FCNX-ray2.35A/B20-377[»]
1FCOX-ray2.20A/B20-377[»]
1FSWX-ray1.90A/B20-376[»]
1FSYX-ray1.75A/B20-376[»]
1GA9X-ray2.10A/B20-377[»]
1I5QX-ray1.83A/B20-377[»]
1IELX-ray2.00A/B20-377[»]
1IEMX-ray2.30A/B20-377[»]
1KDSX-ray2.15A/B20-377[»]
1KDWX-ray2.28A/B20-377[»]
1KE0X-ray2.30A/B20-377[»]
1KE3X-ray2.15A/B20-377[»]
1KE4X-ray1.72A/B20-377[»]
1KVLX-ray1.53A/B20-377[»]
1KVMX-ray2.06A/B20-377[»]
1L0DX-ray1.53A/B20-377[»]
1L0EX-ray1.90A/B20-377[»]
1L0FX-ray1.66A/B20-377[»]
1L0GX-ray1.50A/B20-377[»]
1L2SX-ray1.94A/B20-377[»]
1LL5X-ray1.80A/B20-377[»]
1LL9X-ray1.87A/B20-377[»]
1LLBX-ray1.72A/B20-377[»]
1MXOX-ray1.83A/B20-377[»]
1MY8X-ray1.72A/B20-377[»]
1O07X-ray1.71A/B20-377[»]
1PI4X-ray1.39A/B20-377[»]
1PI5X-ray1.49A/B20-377[»]
1XGIX-ray1.96A/B20-377[»]
1XGJX-ray1.97A/B20-377[»]
2BLSX-ray2.00A/B20-377[»]
2FFYX-ray1.07A/B20-377[»]
2HDQX-ray2.10A/B20-377[»]
2HDRX-ray2.20A/B20-377[»]
2HDSX-ray1.16A/B20-377[»]
2HDUX-ray1.49A/B20-377[»]
2I72X-ray2.20A/B20-377[»]
2P9VX-ray1.80A/B20-377[»]
2PU2X-ray1.86A/B20-377[»]
2PU4X-ray2.00A/B20-377[»]
2R9WX-ray1.80A/B20-377[»]
2R9XX-ray1.90A/B20-377[»]
2RCXX-ray2.00A/B20-377[»]
3BLSX-ray2.30A/B20-377[»]
3BM6X-ray2.10A/B20-377[»]
3FKVX-ray1.85A/B20-377[»]
3FKWX-ray1.50A/B20-377[»]
3GQZX-ray1.80A/B20-377[»]
3GR2X-ray1.80A/B20-377[»]
3GRJX-ray2.49A/B20-377[»]
3GSGX-ray2.10A/B20-377[»]
3GTCX-ray1.90A/B20-377[»]
3GV9X-ray1.80A/B20-377[»]
3GVBX-ray1.80A/B20-377[»]
3IWIX-ray1.64A/B20-377[»]
3IWOX-ray1.90A/B20-377[»]
3IWQX-ray1.84A/B20-377[»]
3IXBX-ray1.63A/B20-377[»]
3IXDX-ray2.64A/B20-377[»]
3IXGX-ray2.14A/B20-377[»]
3IXHX-ray2.30A/B20-377[»]
3O86X-ray1.60A/B20-377[»]
3O87X-ray1.78A/B20-377[»]
3O88X-ray1.64A/B20-377[»]
4E3IX-ray1.60A/B20-377[»]
4E3JX-ray1.80A/B20-377[»]
4E3KX-ray1.43A/B20-377[»]
4E3LX-ray1.43A/B20-377[»]
4E3MX-ray1.44A/B20-377[»]
4E3NX-ray1.49A/B20-377[»]
4E3OX-ray1.60A/B20-377[»]
4JXGX-ray1.65A/B20-377[»]
4JXSX-ray1.90A/B20-377[»]
4JXVX-ray1.76A/B20-377[»]
4JXWX-ray2.30A/B20-377[»]
4KENX-ray1.89B20-377[»]
4KG2X-ray1.89A/B20-377[»]
4KG5X-ray2.11A/B/C/D20-377[»]
4KG6X-ray1.75A/B/C/D20-377[»]
4KZ3X-ray1.67A/B20-377[»]
4KZ4X-ray1.42A/B20-377[»]
4KZ5X-ray1.35A/B20-377[»]
4KZ6X-ray1.68A/B20-377[»]
4KZ7X-ray1.43A/B20-377[»]
4KZ8X-ray2.28A/B20-377[»]
4KZ9X-ray1.72A/B20-377[»]
4KZAX-ray1.60A/B20-377[»]
4KZBX-ray1.37A/B20-377[»]
4LV0X-ray1.65A/B20-377[»]
4LV1X-ray1.74A/B20-377[»]
4LV2X-ray1.65A/B20-377[»]
4LV3X-ray1.42A/B20-377[»]
4OKPX-ray1.37A/B20-377[»]
4OLDX-ray1.48A/B20-377[»]
4OLGX-ray1.71A/B20-377[»]
ProteinModelPortaliP00811.
SMRiP00811. Positions 20-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00811. 1 interaction.
STRINGi511145.b4150.

Chemistry

BindingDBiP00811.
ChEMBLiCHEMBL2026.
DrugBankiDB00456. Cefalotin.
DB01147. Cloxacillin.

Protein family/group databases

MEROPSiS12.006.

2D gel databases

SWISS-2DPAGEP00811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77110; AAC77110; b4150.
BAE78154; BAE78154; BAE78154.
GeneIDi948669.
KEGGiecj:Y75_p4039.
eco:b4150.
PATRICi32123873. VBIEscCol129921_4284.

Organism-specific databases

EchoBASEiEB0038.
EcoGeneiEG10040. ampC.

Phylogenomic databases

eggNOGiCOG1680.
HOGENOMiHOG000267102.
InParanoidiP00811.
KOiK01467.
OMAiMQANINP.
OrthoDBiEOG60SCH1.
PhylomeDBiP00811.

Enzyme and pathway databases

BioCyciEcoCyc:EG10040-MONOMER.
ECOL316407:JW4111-MONOMER.
MetaCyc:EG10040-MONOMER.
BRENDAi3.5.2.6. 2026.
SABIO-RKP00811.

Miscellaneous databases

EvolutionaryTraceiP00811.
PROiP00811.

Gene expression databases

GenevestigatoriP00811.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type."
    Jaurin B., Grundstroem T.
    Proc. Natl. Acad. Sci. U.S.A. 78:4897-4901(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-31.
    Strain: K12.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Overlap between ampC and frd operons on the Escherichia coli chromosome."
    Grundstroem T., Jaurin B.
    Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  7. "Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design."
    Usher K.C., Blaszczak L.C., Weston G.S., Shoichet B.K., Remington S.J.
    Biochemistry 37:16082-16092(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  8. "The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase."
    Powers R.A., Blazquez J., Weston G.S., Morosini M.I., Baquero F., Shoichet B.K.
    Protein Sci. 8:2330-2337(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
  9. "Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design."
    Powers R.A., Caselli E., Focia P.J., Prati F., Shoichet B.K.
    Biochemistry 40:9207-9214(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGUE.
  10. "Structural bases of stability-function tradeoffs in enzymes."
    Beadle B.M., Shoichet B.K.
    J. Mol. Biol. 321:285-296(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS), MUTAGENESIS OF SER-80; LYS-83; TYR-166; ASN-168 AND LYS-331.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).

Entry informationi

Entry nameiAMPC_ECOLI
AccessioniPrimary (citable) accession number: P00811
Secondary accession number(s): Q2M6F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 27, 2015
This is version 150 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.