KEGG   Clavibacter michiganensis subsp. michiganensis: CMM_0514
Entry
CMM_0514          CDS       T00529                                 
Symbol
pheA
Name
(GenBank) Prephenate dehydratase (|NP_628146.1| prephenate dehydratase [Streptomyces coelicolor A3(2)]; ZP_00058942.1| COG0077: Prephenate dehydratase [Thermobifida fusca]). pfam00800, PDT, Prephenate dehydratase. This protein is involved in Phenylalanine biosynthesis. This protein catalyses the decarboxylation of prephenate to phenylpyruvate. pfam01842, ACT, ACT domain. This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme.; High confidence in function and specificity
  KO
K04518  prephenate dehydratase [EC:4.2.1.51]
Organism
cmi  Clavibacter michiganensis subsp. michiganensis
Pathway
cmi00400  Phenylalanine, tyrosine and tryptophan biosynthesis
cmi01100  Metabolic pathways
cmi01110  Biosynthesis of secondary metabolites
cmi01230  Biosynthesis of amino acids
Brite
KEGG Orthology (KO) [BR:cmi00001]
 09100 Metabolism
  09105 Amino acid metabolism
   00400 Phenylalanine, tyrosine and tryptophan biosynthesis
    CMM_0514 (pheA)
Enzymes [BR:cmi01000]
 4. Lyases
  4.2  Carbon-oxygen lyases
   4.2.1  Hydro-lyases
    4.2.1.51  prephenate dehydratase
     CMM_0514 (pheA)
SSDB
Motif
Pfam: PDT ACT
Other DBs
NCBI-ProteinID: CAN00538
UniProt: A5CNA1
LinkDB
Position
599010..599966
AA seq 318 aa
MAETPRPDETYSYLGPSGTFTEAALKQVEAARGRTWRAVNNASEALADVVSGTSVAAMIA
IENSVEGGVTATQDALANIPGLRILSEHLVPVTFDLVVRPGTALADVRTVAAHPVAYGQC
RRFLERELPTHGHVPASSNVAAALSLLDGGIADAAIAPPQITESQPLEAVARGIGDNPNA
VTRFVLVGRATTLPQRTGADKTSLIVELPDDRAGSLLDLLEQFATRGVNLTLIQSRPIGD
ALGRYRFVIDAEGHVRDERVADALLGIRRFSPRVTFLGSYPRADGTPSTYRARYEDDVFL
EARDWLRGIVSAEPGAGD
NT seq 957 nt   +upstreamnt  +downstreamnt
atggccgagaccccgcgacccgacgagacgtacagctacctcgggccgtcgggcaccttc
acggaggcagcgctcaagcaggtggaggccgctcgcgggcgcacgtggcgcgcggtgaac
aacgcctcggaggccctcgccgacgtcgtgtccggcacctcggtcgccgccatgatcgcc
atcgagaactccgtcgagggcggggtgacggccacgcaggacgcgctcgcgaacatcccg
gggctgcggatcctcagcgagcacctcgtgccggtgacgttcgacctcgtggtgcggccg
ggtaccgcgctcgccgacgtgcgcacggtcgccgcgcaccccgtcgcctacggccagtgc
cgccgcttcctcgagcgcgagcttcccacgcacgggcacgtgcccgcgtcctcgaacgtg
gccgcggcgctgtccctgctggacggcgggatcgcggacgccgccatcgcgcccccgcag
atcacggagagccagccgctcgaggccgtcgcccgcggcatcggcgacaacccgaacgcc
gtcacgcgcttcgtgctcgtcggccgcgcgaccacgctgccgcagcgcacgggcgccgac
aagacgagcctcatcgtcgagctgcccgacgaccgcgccggatccctgctcgacctcctg
gagcagttcgcgacccgcggggtgaacctcacgctcatccagtcgcggcccatcggcgac
gcgctcggccgctaccggttcgtcatcgacgcggaggggcacgtgcgcgacgagcgcgtg
gccgacgccctgctcgggatccgccgcttcagcccgcgcgtcaccttcctcggctcgtac
ccccgggccgacggcacgcccagcacctaccgcgcgcggtacgaggacgacgtcttcctc
gaggcgcgcgactggctgcgcggcatcgtctcggccgagccaggcgcgggcgactga

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