Delta-aminolevulinic acid dehydratase
Details
- Name
- Delta-aminolevulinic acid dehydratase
- Synonyms
- 4.2.1.24
- ALAD
- Porphobilinogen synthase
- Gene Name
- hemB
- Organism
- Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
- Amino acid sequence
>lcl|BSEQ0010895|Delta-aminolevulinic acid dehydratase MSFTPANRAYPYTRLRRNRRDDFSRRLVRENVLTVDDLILPVFVLDGVNQRESIPSMPGV ERLSIDQLLIEAEEWVALGIPALALFPVTPVEKKSLDAAEAYNPEGIAQRATRALRERFP ELGIITDVALDPFTTHGQDGILDDDGYVLNDVSIDVLVRQALSHAEAGAQVVAPSDMMDG RIGAIREALESAGHTNVRIMAYSAKYASAYYGPFRDAVGSASNLGKGNKATYQMDPANSD EALHEVAADLAEGADMVMVKPGMPYLDIVRRVKDEFRAPTFVYQVSGEYAMHMGAIQNGW LAESVILESLTAFKRAGADGILTYFAKQAAEQLRRGR
- Number of residues
- 337
- Molecular Weight
- 37036.6
- Theoretical pI
- 4.83
- GO Classification
- Functionsporphobilinogen synthase activity / zinc ion bindingProcessesheme biosynthetic process / porphyrin-containing compound biosynthetic process / protoporphyrinogen IX biosynthetic processComponentscytosol
- General Function
- Zinc ion binding
- Specific Function
- Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
- Pfam Domain Function
- ALAD (PF00490)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0010896|Delta-aminolevulinic acid dehydratase (hemB) GTGAGCTTCACTCCCGCCAATCGCGCCTATCCCTACACCCGCCTGCGGCGCAATCGCCGC GATGACTTCTCCCGCCGCCTGGTCCGCGAGAATGTCCTCACCGTCGACGACCTGATCCTG CCGGTGTTCGTCCTCGATGGGGTCAACCAGCGTGAAAGCATTCCGTCGATGCCCGGCGTC GAGCGCCTGTCCATCGACCAGTTGCTGATCGAGGCGGAAGAGTGGGTGGCCCTGGGCATT CCGGCGCTGGCGCTGTTCCCTGTGACCCCGGTGGAGAAGAAGTCCCTGGACGCCGCCGAG GCATACAACCCGGAAGGCATCGCCCAGCGCGCCACCCGTGCCCTGCGCGAGCGCTTTCCG GAGCTGGGCATCATCACCGACGTGGCGCTCGACCCGTTCACCACCCATGGCCAGGACGGC ATCCTGGATGACGATGGCTACGTCCTCAACGACGTCAGCATCGACGTGCTGGTACGGCAG GCGCTGTCCCACGCCGAGGCCGGCGCCCAGGTGGTAGCGCCCTCGGACATGATGGACGGT CGCATCGGTGCGATCCGCGAGGCCCTGGAGTCTGCCGGCCACACCAATGTGCGGATCATG GCCTACTCGGCCAAGTACGCCAGCGCCTACTACGGTCCGTTCCGCGATGCGGTCGGCTCG GCTTCGAACCTCGGCAAGGGCAACAAGGCCACCTACCAGATGGATCCGGCGAACAGCGAC GAGGCACTTCACGAAGTGGCCGCCGACCTGGCCGAAGGCGCCGACATGGTGATGGTCAAG CCGGGCATGCCCTACCTCGACATCGTGCGTCGGGTGAAGGATGAATTCCGCGCCCCGACC TTTGTCTACCAGGTCAGCGGCGAGTATGCGATGCACATGGGCGCCATCCAGAACGGCTGG CTGGCCGAATCGGTGATCCTCGAATCCCTTACCGCCTTCAAACGTGCCGGCGCCGATGGC ATTCTGACCTACTTCGCCAAGCAGGCCGCAGAACAATTAAGACGGGGGCGTTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q59643 UniProtKB Entry Name HEM2_PSEAE GenBank Protein ID 1009431 GenBank Gene ID X91820 - General References
- Frankenberg N, Kittel T, Hungerer C, Romling U, Jahn D: Cloning, mapping and functional characterization of the hemB gene of Pseudomonas aeruginosa, which encodes a magnesium-dependent 5-aminolevulinic acid dehydratase. Mol Gen Genet. 1998 Feb;257(4):485-9. [Article]
- Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV: Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature. 2000 Aug 31;406(6799):959-64. [Article]
- Frankenberg N, Erskine PT, Cooper JB, Shoolingin-Jordan PM, Jahn D, Heinz DW: High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase. J Mol Biol. 1999 Jun 11;289(3):591-602. [Article]
- Frere F, Schubert WD, Stauffer F, Frankenberg N, Neier R, Jahn D, Heinz DW: Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism. J Mol Biol. 2002 Jul 5;320(2):237-47. [Article]
- Frere F, Nentwich M, Gacond S, Heinz DW, Neier R, Frankenberg-Dinkel N: Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors. Biochemistry. 2006 Jul 11;45(27):8243-53. [Article]
- Heinemann IU, Schulz C, Schubert WD, Heinz DW, Wang YG, Kobayashi Y, Awa Y, Wachi M, Jahn D, Jahn M: Structure of the heme biosynthetic Pseudomonas aeruginosa porphobilinogen synthase in complex with the antibiotic alaremycin. Antimicrob Agents Chemother. 2010 Jan;54(1):267-72. doi: 10.1128/AAC.00553-09. Epub 2009 Oct 12. [Article]