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CDS information : Ovied_00200


close this sectionLocation

Organism
StrainATCC 11891
Entry nameOviedomycin
Contig
Start / Stop / Direction20,498 / 22,216 / + [in whole cluster]
20,498 / 22,216 / + [in contig]
Location20498..22216 [in whole cluster]
20498..22216 [in contig]
TypeCDS
Length1,719 bp (572 aa)
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close this sectionAnnotation

Category2.1 modification addition of extender units
Productacyl-CoA carboxylase alpha subunit
Product (GenBank)acetyl-CoA carboxylase complex, alpha-chain
Gene
Gene (GenBank)ovmH
EC number6.4.1.-
Keyword
  • malonyl-CoA
Note
Note (GenBank)
Reference
ACC
PmId
[15368568] Genetic organization of the biosynthetic gene cluster for the antitumor angucycline oviedomycin in Streptomyces antibioticus ATCC 11891. (Chembiochem. , 2004)
[12027768] Oviedomycin, an unusual angucyclinone encoded by genes of the oleandomycin-producer Streptomyces antibioticus ATCC11891. (J Nat Prod. , 2002)
[24148183] Engineering precursor metabolite pools for increasing production of antitumor mithramycins in Streptomyces argillaceus. (Metab Eng. , 2013)
Related Reference
ACC
Q9RGQ6
PmId
[10589718] Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). (Microbiology. , 1999)
ACC
Q9X4K6
PmId
[10589718] Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). (Microbiology. , 1999)

close this sectionSequence

selected fasta
>acyl-CoA carboxylase alpha subunit [acetyl-CoA carboxylase complex, alpha-chain]
MSLRKVLIANRGEIAVRVARACRDAGIASVAVYADPDRDAVHVRAADEAFALGGDTPATS
YLDIEKVLLAAKQSGADAIHPGYGFLSENAEFAQAVLDAGLIWIGPPPQAIRDLGDKVAA
RHIAQRAGAPLVAGTPDPVSGAEEVVAFAEEHGLPIAIKAAFGGGGRGLKVARTLEEVPE
LYESAVREAVAAFGRGECFVERYLDRPRHVETQCLADKHGNVVVVSTRDCSLQRRHQKLV
EEAPAPFLSEEQMAELYRASKAILKEAGYEGAGTCEFLVGQDGTISFLEVNTRLQVEHPV
TEEVAGIDLVREMFRIADGEPLGYDDPVLRGHSFEFRINGEDPGVRLDAGVEAGSVIGPA
WDSLLAKLIVTGRTRKEALQRAARALEEFRVEGMATAIPFHRKVVTDPAFAPELTGSSEP
FTVHTRWIETEFVNDIKPFTAPADAEADEDAARETVVVEVGGKRLEVSLPSSLGMSLART
GLAAGAKPKRRAAKKSGPVASGDTLTSPMQGTIVKIAVEEGQQVKEGDLVVVLEAMKMEQ
PLNAHKAGTIKGLTAEVGASLTSGAAICEITD
selected fasta
>acyl-CoA carboxylase alpha subunit [acetyl-CoA carboxylase complex, alpha-chain]
ATGAGTCTGCGCAAGGTGCTCATCGCCAACCGTGGCGAAATCGCTGTCCGCGTGGCCCGG
GCCTGCCGGGACGCCGGGATCGCGAGCGTGGCCGTCTACGCCGACCCGGACCGCGACGCT
GTGCACGTACGGGCCGCCGACGAGGCGTTCGCGCTGGGGGGTGACACCCCGGCCACCAGC
TACCTGGACATCGAGAAGGTGCTGCTGGCCGCCAAGCAGTCCGGTGCGGACGCGATCCAC
CCCGGCTACGGCTTCCTGTCCGAGAACGCCGAGTTCGCCCAGGCCGTTCTCGACGCGGGC
CTGATCTGGATCGGCCCGCCGCCGCAGGCGATCCGGGACCTGGGTGACAAGGTCGCCGCC
CGTCACATCGCCCAGCGCGCCGGCGCCCCGCTGGTGGCGGGTACGCCGGACCCGGTGAGT
GGTGCGGAGGAGGTCGTGGCTTTCGCCGAGGAGCACGGTCTGCCGATCGCGATCAAGGCC
GCGTTCGGCGGCGGCGGGCGCGGTCTGAAGGTCGCCCGCACCCTCGAAGAGGTCCCCGAG
CTGTACGAGTCCGCCGTGCGTGAGGCCGTCGCCGCGTTCGGCCGTGGCGAGTGCTTCGTC
GAGCGCTACCTCGACCGGCCGCGGCATGTGGAGACGCAGTGCCTGGCCGACAAGCACGGC
AACGTCGTCGTGGTCTCCACCCGCGACTGCTCCCTGCAGCGCCGTCACCAGAAACTGGTC
GAGGAGGCTCCCGCACCGTTCCTGTCCGAGGAGCAGATGGCGGAGCTGTACCGGGCGTCG
AAGGCCATCCTGAAGGAGGCCGGGTACGAGGGCGCGGGCACGTGTGAGTTCCTGGTCGGG
CAGGACGGCACGATCTCCTTCCTGGAGGTCAACACCCGCCTGCAGGTCGAGCACCCGGTC
ACCGAGGAAGTCGCCGGCATCGACCTGGTCCGGGAGATGTTCCGCATCGCCGACGGCGAA
CCCCTCGGCTACGACGACCCGGTGCTGCGCGGTCACTCCTTCGAGTTCCGTATCAACGGT
GAGGACCCGGGCGTGCGTCTGGACGCGGGCGTGGAGGCCGGCAGTGTGATCGGCCCGGCG
TGGGACTCCCTGCTGGCCAAGCTGATCGTCACCGGCCGCACCCGCAAGGAAGCCCTCCAG
CGGGCCGCCCGCGCGCTGGAGGAGTTCCGTGTCGAGGGCATGGCCACCGCCATCCCCTTC
CACCGCAAGGTCGTCACCGACCCCGCCTTCGCCCCCGAACTCACCGGCTCCAGCGAGCCG
TTCACGGTCCACACCCGGTGGATCGAGACCGAGTTCGTCAACGACATCAAGCCCTTCACC
GCCCCCGCCGACGCCGAGGCCGACGAGGATGCGGCGCGTGAGACGGTCGTGGTCGAGGTC
GGCGGCAAGCGCCTGGAGGTCTCCCTGCCCTCCAGCCTGGGCATGAGCCTGGCCCGCACC
GGGCTCGCGGCCGGGGCCAAGCCCAAGCGGCGCGCGGCGAAGAAGTCCGGGCCCGTCGCC
TCCGGCGACACCCTGACCTCCCCCATGCAGGGCACCATCGTCAAGATCGCCGTCGAGGAA
GGCCAGCAGGTCAAGGAGGGCGACCTGGTCGTCGTCCTGGAGGCCATGAAGATGGAACAG
CCCCTCAACGCCCACAAGGCGGGCACCATCAAGGGCCTGACCGCCGAGGTCGGCGCCTCC
CTCACCTCCGGCGCCGCCATCTGCGAGATCACGGACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR000089 Biotin/lipoyl attachment (Domain)
 [504-570]  4.70000000000001e-17 PF00364
PF00364   Biotin_lipoyl
 [503-570]  PS50968
PS50968   BIOTINYL_LIPOYL
IPR001882 Biotin-binding site (Binding_site)
 [527-544]  PS00188
PS00188   BIOTIN
IPR005479 Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain (Domain)
 [116-322]  2.20000000000002e-74 PF02786
PF02786   CPSase_L_D2
 [287-294]  PS00867
PS00867   CPSASE_2
IPR005481 Carbamoyl-phosphate synthase, large subunit, N-terminal (Domain)
 [3-111]  6.09999999999996e-41 PF00289
PF00289   CPSase_L_chain
IPR005482 Biotin carboxylase, C-terminal (Domain)
 [336-429]  4.29999999999999e-22 PF02785
PF02785   Biotin_carb_C
 [335-429]  5.79999653854781e-36 SM00878
SM00878   Biotin_carb_C
IPR005483 Carbamoyl-phosphate synthase large subunit, CPSase domain (Domain)
 [158-170]  3.79999862644791e-05 PR00098 [198-217]  3.79999862644791e-05 PR00098 [287-316]  3.79999862644791e-05 PR00098 [364-382]  3.79999862644791e-05 PR00098
PR00098   CPSASE
IPR011053 Single hybrid motif (Domain)
 [488-571]  4.49999046578037e-19 SSF51230
SSF51230   Hybrid_motif
IPR011054 Rudiment single hybrid motif (Domain)
 [330-432]  2.70000183580794e-28 SSF51246
SSF51246   Rudmnt_hyb_motif
IPR011761 ATP-grasp fold (Domain)
 [121-318]  PS50975
PS50975   ATP_GRASP
IPR011764 Biotin carboxylation domain (Domain)
 [2-425]  PS50979
PS50979   BC
IPR013815 ATP-grasp fold, subdomain 1 (Domain)
 [131-203]  3.7e-21 G3DSA:3.30.1490.20
G3DSA:3.30.1490.20   ATP_grasp_subdomain_1
IPR013816 ATP-grasp fold, subdomain 2 (Domain)
 [205-431]  4.89999999999996e-75 G3DSA:3.30.470.20
G3DSA:3.30.470.20   ATP_grasp_subdomain_2
IPR016185 Pre-ATP-grasp fold (Domain)
 [1-114]  9.49996855930963e-48 SSF52440
SSF52440   PreATP-grasp-like
 [3-130]  1.99999999999999e-48 G3DSA:3.40.50.20
G3DSA:3.40.50.20   Pre-ATP_grasp
SignalP
 [1-27]  0.253 Signal
Bacteria, Gram-positive   
TMHMM No significant hit