UniProtKB - A5JTM6 (CBACL_PSEUC)
4-chlorobenzoate--CoA ligase
Functioni
Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoyl is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA. Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-methylbenzoate also act as substrates. Inactive towards 4-aminobenzoate, 4-hydroxybenzoate, 2-aminobenzoate, 2,3-dihydroxybenzoate, 4-coumarate and the aliphatic carboxylic acids palmate, caproate, laurate and butyrate. Negligible activity is detected when ATP is replaced by UTP, CTP or GTP as cosubstrate.
3 PublicationsCatalytic activityi
- EC:6.2.1.333 Publications
Cofactori
Activity regulationi
Kineticsi
- KM=8.5 µM for 4-chlorobenzoate3 Publications
- KM=70 µM for CoA3 Publications
- KM=104 µM for ATP (with magnesium as cofactor)3 Publications
- KM=43 µM for ATP (with manganese as cofactor)3 Publications
- KM=59 µM for ATP (with cobalt as cofactor)3 Publications
- KM=15 µM for 4-bromobenzoate3 Publications
- KM=17 µM for 4-iodobenzoate3 Publications
- KM=700 µM for benzoate3 Publications
- KM=130 µM for 4-methylbenzoate3 Publications
pH dependencei
Temperature dependencei
: 4-chlorobenzoate degradation Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes 4-hydroxybenzoate from 4-chlorobenzoate.1 Publication This subpathway is part of the pathway 4-chlorobenzoate degradation, which is itself part of Xenobiotic degradation.View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-hydroxybenzoate from 4-chlorobenzoate, the pathway 4-chlorobenzoate degradation and in Xenobiotic degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 409 | ATPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 161 – 169 | ATPBy similarity | 9 | |
Nucleotide bindingi | 300 – 305 | ATPBy similarity | 6 |
GO - Molecular functioni
- 4-chlorobenzoate-CoA ligase activity Source: UniProtKB
- ATP binding Source: UniProtKB-KW
Keywordsi
Molecular function | Ligase |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
SABIO-RKi | A5JTM6 |
UniPathwayi | UPA01011;UER01021 |
Names & Taxonomyi
Protein namesi | Recommended name: 4-chlorobenzoate--CoA ligase2 Publications (EC:6.2.1.33)Short name: 4-CBA:CoA ligaseImported |
Organismi | Pseudomonas sp. (strain CBS-3) |
Taxonomic identifieri | 72586 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 163 | G → I: Significantly inhibits the adenylation part of the reaction. 1 Publication | 1 | |
Mutagenesisi | 166 | G → I: Significantly inhibits the adenylation part of the reaction. 1 Publication | 1 | |
Mutagenesisi | 168 | P → A: No catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 169 | K → M: Significantly inhibits the adenylation part of the reaction. 1 Publication | 1 | |
Mutagenesisi | 306 | E → Q: Significantly inhibits the adenylation part of the reaction. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000401169 | 1 – 528 | 4-chlorobenzoate--CoA ligaseAdd BLAST | 528 |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsFamily & Domainsi
Sequence similaritiesi
Family and domain databases
Gene3Di | 3.30.300.30, 1 hit |
InterProi | View protein in InterPro IPR025110, AMP-bd_C IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF13193, AMP-binding_C, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MQTVHEMLRR AVSRVPHRWA IVDAARSTFD ICRTGETSRN EGSATARLWP
60 70 80 90 100
QPARPLAVVS GNSVEAVIAV LALHRLQAVP ALMNPRLKPA EISELVARGE
110 120 130 140 150
MARAVVANDA GVMEAIRTRV PSVCVLALDD LVSGSRVPEV AGKSLPPPPC
160 170 180 190 200
EPEQAGFVFY TSGTTGLPKG AVIPQRAAES RVLFMATQAG LRHGSHNVVL
210 220 230 240 250
GLMPLYHTIG FFAVLVAAMA FDGTYVVVEE FDAGNVLKLI ERERVTAMFA
260 270 280 290 300
TPTHLDALTT AVEQAGARLE SLEHVTFAGA TMPDTVLERV NRFIPGEKVN
310 320 330 340 350
IYGTTEAMNS LYMRAVRIAG TVMRPGFFSE VRIVRVGGDV DDGCPTVKRA
360 370 380 390 400
SWRWRRRMRP FQATLTNLRL LQKSFRKAGT GRAICVRDGS GNIVVLGRVD
410 420 430 440 450
DMIISGGENI HPSEVERILA AAPGVAEVVV IGVKDERWGQ SVVACVVLQP
460 470 480 490 500
GASASAERLD AFCRASALAD FKRPRRYVFL DELPKSAMNK VLRRQLMQHV
510 520
SATSSAAVVP APAVKQRTYA PSGRAIAR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | EF569604 Genomic DNA Translation: ABQ44579.1 |
Genome annotation databases
KEGGi | ag:ABQ44579 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | EF569604 Genomic DNA Translation: ABQ44579.1 |
3D structure databases
SMRi | A5JTM6 |
ModBasei | Search... |
Genome annotation databases
KEGGi | ag:ABQ44579 |
Enzyme and pathway databases
UniPathwayi | UPA01011;UER01021 |
SABIO-RKi | A5JTM6 |
Family and domain databases
Gene3Di | 3.30.300.30, 1 hit |
InterProi | View protein in InterPro IPR025110, AMP-bd_C IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF13193, AMP-binding_C, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CBACL_PSEUC | |
Accessioni | A5JTM6Primary (citable) accession number: A5JTM6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 30, 2010 |
Last sequence update: | June 26, 2007 | |
Last modified: | February 23, 2022 | |
This is version 39 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families