4-chlorobenzoyl CoA ligase
Details
- Name
- 4-chlorobenzoyl CoA ligase
- Synonyms
- Not Available
- Gene Name
- Not Available
- Organism
- Alcaligenes sp. AL3007
- Amino acid sequence
>lcl|BSEQ0022065|4-chlorobenzoyl CoA ligase MQTVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADGLRPQQRVAVV APNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRGEMTAAVIAVGRQVADAIFQS GSGARIIFLGDLVRDGEPYSYGPPIEDPQREPAQPAFIFYTSGTTGLPKAAIIPQRAAES RVLFMSTQVGLRHGRHNVVLGLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLV QQEQVTSLFATPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEK VNIYGTTEAMNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGVDEIVANGEEGELIVAASDS AFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGRVDDMIISGGENIHPSEIERV LGTAPGVTEVVVIGLADQRWGQSVTACVVPRLGETLSADALDTFCRSSELADFKRPKRYF ILDQLPKNALNKVLRRQLVQQVSS
- Number of residues
- 504
- Molecular Weight
- 54319.855
- Theoretical pI
- 6.68
- GO Classification
- Functionsligase activity / metal ion binding / nucleotide bindingComponentsintegral component of membrane
- General Function
- Nucleotide binding
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- 198-221
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0006187|1506 bp ATGCAGACAGTCAATGAGATGCTCCGCCGGGCAGCCACCCGCGCGCCAGATCACTGCGCG TTGGCGGTCCCGGCACGTGGGCTCCGTCTAACGCACGCAGAGCTACGGGCGCGGGTGGAA GCTGTGGCCGGCCTGCATGCAGACGGGCTTCGGCCGCAGCAGAGGGTCGCGGTGGTCGCC CCAAATTCCGCCGACGTGGTCATTGCAATCCTCGCGTTGCATCGGCTCGCAGTTCCTGCG CTTCTCAATCCGCGTCTGAAGTCCGCTGAACTTGCCGAGCTCATCAAGCGCGGGGAAATG ACGGCTGCCGTCATAGCTGTCGGCCGGCAGGTGGCGGATGCCATTTTCCAGAGCGGCAGC GGAGCGCGAATCATTTTTCTCGGCGACTTGGTACGTGATGGGGAGCCTTACTCCTATGGT CCTCCGATTGAGGATCCGCAGCGCGACGCAGCGCAGCCGGCGTTCATCTTCTATACCTCG GGAACCACCGGCCTGCCTAAGGCCGCGATCATTCCGCAGCGAGCTGCGGAAAGTCGAGTG CTGTTCATGTCGACGCAGGTCGGATTGCGTCACGGACGGCACAACGTGGTGCTGGGTCTG ATGCCGCTCTACCACGTGGTCGGCTTCTTCGCTGTCCTGGTCGCCGCACTCGCTCTCGAT GGCACCTATGTCGTAGTAGAGGAATTCCGACCCGTGGATGCGCTCCAGCTCGTGCAACAG GAGCAGGTCACATCGCTATTCGCGACGCCAACGCACCTCGATGCGCTGGCCGCCGCAGCG CACGCTGGCTCGAGCCTCAAACTGGATTCGTTGCGCCACGTCACATTCGCGGGTGCGACC ATGCCCGATGCCGTGCTCGAGACCGTTCACCAGCATCTGCCCGGCGAGAAAGTGAACATC TACGGCACTACTGAGGCGATGAACTCGCTCTACATGCGACACGCGAAGACGGGTACCGAA ATGGCGCCTGGGTTCTTCTCGGAAGTGCGGATAGTTCGTATCGGCGGCGGTGTCGACGAG ATAGTGGCCAACGGAGAAGAGGGGGAGCTGATCGTGGCCGCCTCTGATTCAGCCTTCGTC GGTTACTTGAACCAGCCCCAAGCAACTGCGGAAAAGCTGCAGGACGGGTGGTATAGGACC AGCGACGTTGCCGTGTGGACACCTGAAGGTACCGTTCGAATCCTCGGTCGGGTGGACGAC ATGATCATCTCCGGCGGCGAGAACATTCACCCGTCCGAAATCGAGCGCGTGCTCGGAACC GCACCAGGCGTGGCTGAGGTAGTCGTGATTGGCCTCGCAGACCAGCGGTGGGGGCAGTCT GTGACTGCCTGTGTTGTCCCCCGGCTTGGAGAGACCCTATCCGCAGATGCGCTCGACACT TTCTGCCGCTCCAGTGAGCTTGCTGATTTCAAGCGGCCCAAGCGCTACTTCATCTTGGAT CAGCTCCCGAAGAATGCATTAAACAAGGTACTGCGGCGCCACGTGGTGCAGCAGGTGTCA AGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q8GN86 UniProtKB Entry Name Q8GN86_9BURK GenBank Gene ID AF537222 - General References
- Gulick AM, Lu X, Dunaway-Mariano D: Crystal structure of 4-chlorobenzoate:CoA ligase/synthetase in the unliganded and aryl substrate-bound states. Biochemistry. 2004 Jul 13;43(27):8670-9. [Article]
- Wu R, Reger AS, Cao J, Gulick AM, Dunaway-Mariano D: Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range. Biochemistry. 2007 Dec 18;46(50):14487-99. Epub 2007 Nov 21. [Article]
- Reger AS, Wu R, Dunaway-Mariano D, Gulick AM: Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase. Biochemistry. 2008 Aug 5;47(31):8016-25. doi: 10.1021/bi800696y. Epub 2008 Jul 12. [Article]
- Wu R, Reger AS, Lu X, Gulick AM, Dunaway-Mariano D: The mechanism of domain alternation in the acyl-adenylate forming ligase superfamily member 4-chlorobenzoate: coenzyme A ligase. Biochemistry. 2009 May 19;48(19):4115-25. doi: 10.1021/bi9002327. [Article]