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Protein
Submitted name:

4-chlorobenzoyl CoA ligase

Gene
N/A
Organism
Alcaligenes sp. AL3007
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei161 – 1611AMPCombined sources
Binding sitei385 – 3851AMPCombined sources
Binding sitei400 – 4001AMPCombined sources
Binding sitei411 – 4111AMPCombined sources
Metal bindingi483 – 4831CalciumCombined sources
Metal bindingi484 – 4841CalciumCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi281 – 2822AMPCombined sources
Nucleotide bindingi302 – 3032AMPCombined sources
Nucleotide bindingi307 – 3082AMPCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

LigaseImported

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BRENDAi6.2.1.33. 236.

Names & Taxonomyi

Protein namesi
Submitted name:
4-chlorobenzoyl CoA ligaseImported
Encoded oniPlasmid pss70Imported
OrganismiAlcaligenes sp. AL3007Imported
Taxonomic identifieri206162 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAlcaligenes

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei198 – 22124HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T5DX-ray2.21X1-42[»]
X44-77[»]
X79-258[»]
X260-504[»]
1T5HX-ray2.00X1-42[»]
X44-77[»]
X79-258[»]
X260-504[»]
2QVXX-ray2.70X1-504[»]
2QVYX-ray2.76X1-504[»]
2QVZX-ray2.50X1-504[»]
2QW0X-ray2.56X1-504[»]
3CW8X-ray2.25X1-504[»]
3CW9X-ray2.00A/B1-504[»]
3DLPX-ray2.60X1-504[»]
ProteinModelPortaliQ8GN86.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GN86.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 407399AMP-bindingInterPro annotationAdd
BLAST
Domaini416 – 49176AMP-binding_CInterPro annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8GN86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTVNEMLRR AATRAPDHCA LAVPARGLRL THAELRARVE AVAARLHADG
60 70 80 90 100
LRPQQRVAVV APNSADVVIA ILALHRLGAV PALLNPRLKS AELAELIKRG
110 120 130 140 150
EMTAAVIAVG RQVADAIFQS GSGARIIFLG DLVRDGEPYS YGPPIEDPQR
160 170 180 190 200
EPAQPAFIFY TSGTTGLPKA AIIPQRAAES RVLFMSTQVG LRHGRHNVVL
210 220 230 240 250
GLMPLYHVVG FFAVLVAALA LDGTYVVVEE FRPVDALQLV QQEQVTSLFA
260 270 280 290 300
TPTHLDALAA AAAHAGSSLK LDSLRHVTFA GATMPDAVLE TVHQHLPGEK
310 320 330 340 350
VNIYGTTEAM NSLYMRQPKT GTEMAPGFFS EVRIVRIGGG VDEIVANGEE
360 370 380 390 400
GELIVAASDS AFVGYLNQPQ ATAEKLQDGW YRTSDVAVWT PEGTVRILGR
410 420 430 440 450
VDDMIISGGE NIHPSEIERV LGTAPGVTEV VVIGLADQRW GQSVTACVVP
460 470 480 490 500
RLGETLSADA LDTFCRSSEL ADFKRPKRYF ILDQLPKNAL NKVLRRQLVQ

QVSS
Length:504
Mass (Da):54,320
Last modified:November 13, 2013 - v2
Checksum:iDA584783EB917A6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF537222 Genomic DNA. Translation: AAN10109.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF537222 Genomic DNA. Translation: AAN10109.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T5DX-ray2.21X1-42[»]
X44-77[»]
X79-258[»]
X260-504[»]
1T5HX-ray2.00X1-42[»]
X44-77[»]
X79-258[»]
X260-504[»]
2QVXX-ray2.70X1-504[»]
2QVYX-ray2.76X1-504[»]
2QVZX-ray2.50X1-504[»]
2QW0X-ray2.56X1-504[»]
3CW8X-ray2.25X1-504[»]
3CW9X-ray2.00A/B1-504[»]
3DLPX-ray2.60X1-504[»]
ProteinModelPortaliQ8GN86.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi6.2.1.33. 236.

Miscellaneous databases

EvolutionaryTraceiQ8GN86.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU."
    Zhuang Z., Gartemann K.H., Eichenlaub R., Dunaway-Mariano D.
    Appl. Environ. Microbiol. 69:2707-2711(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: AL3007Imported.
    Plasmid: pss70
  2. "Crystal structure of 4-chlorobenzoate:CoA ligase/synthetase in the unliganded and aryl substrate-bound states."
    Gulick A.M., Lu X., Dunaway-Mariano D.
    Biochemistry 43:8670-8679(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-42; 44-77; 79-258 AND 260-504 IN COMPLEX WITH CALCIUM.
  3. Yoshinaga K.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: AL3007Imported.
    Plasmid: pss70
  4. "Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range."
    Wu R., Reger A.S., Cao J., Gulick A.M., Dunaway-Mariano D.
    Biochemistry 46:14487-14499(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
  5. "Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase."
    Reger A.S., Wu R., Dunaway-Mariano D., Gulick A.M.
    Biochemistry 47:8016-8025(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH AMP.
  6. "The mechanism of domain alternation in the acyl-adenylate forming ligase superfamily member 4-chlorobenzoate: coenzyme A ligase."
    Wu R., Reger A.S., Lu X., Gulick A.M., Dunaway-Mariano D.
    Biochemistry 48:4115-4125(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).

Entry informationi

Entry nameiQ8GN86_9BURK
AccessioniPrimary (citable) accession number: Q8GN86
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: November 13, 2013
Last modified: May 11, 2016
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, PlasmidImported

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.