Chro_00060 Chro_00060   Chro_00080 Chro_00080

Chro_00070 : CDS information

close this sectionLocation

Organism
StrainATCC 13273 (=NBRC 3746)
Entry nameChromomycin
Contig
Start / Stop / Direction5,703 / 8,102 / + [in whole cluster]
5,703 / 8,102 / + [in contig]
Location5703..8102 [in whole cluster]
5703..8102 [in contig]
TypeCDS
Length2,400 bp (799 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative biotin carboxylase/putative oxidoreductase
Product (GenBank)oxygenase
Gene
Gene (GenBank)cmmOI
EC number
Keyword
Note
  • The N-terminal position was modified from original INSDC entry.
  • bifunctional protein
Note (GenBank)
Reference
ACC
PmId
[15112992] Biosynthesis of the antitumor chromomycin A3 in Streptomyces griseus: analysis of the gene cluster and rational design of novel chromomycin analogs. (Chem Biol. , 2004)
comment
aureolic acid type antitumor drug chromomycin A3の生合成gene clusterの同定論文。

CmmOI : Oxygenase

配列解析から機能推定。
MtmOI oxygenaseと似ている。
N末にbiotin carboxylasesに似た領域がfusionしている。
Related Reference
ACC
P49787
PmId
[7592499] The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis. (J Bacteriol. , 1995)
comment
>for N-terminal side

Blast id43.82%, 4e-54
B.subtilis_accC1
Biotin carboxylase 1(EC 6.3.4.14)
synonym: Acetyl-CoA carboxylase subunit A 1(EC 6.4.1.2)

Acetyl-CoA carboxylaseはBiotin carboxylase(BC, accC), carboxyl transferase(CT, accA and accD), biotin carboxyl carrier protein(BCCP, accB)から構成され、ATPを使ってacetyl-CoAをカルボキシル化しmalonyl-CoAを合成する。

accBとaccCをクローニング、シークエンス。
オペロンになっている。
ACC
Q70DW2
NITE
Resis_00160
PmId
[17090047] The boat-shaped polyketide resistoflavin results from re-facial central hydroxylation of the discoid metabolite resistomycin. (J Am Chem Soc. , 2006)
comment
>for C-terminal side

Blast id30.18%, 2e-35
Streptomyces resistomycificus_remO
RemO protein
[DoBISCUIT]resistomycin hydroxylase

resistomycin→resistoflavinへの珍しいenantioface-differentiating hydroxylationが、FAD-dependent monooxygenase_RemOによって触媒されるということをvivoとvitroの実験で実証している。
ACC
Q3S8R0
NITE
Oxtet_00060
PmId
[18422316] Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. (J Am Chem Soc. , 2008)
[19472250] Identification of OxyE as an ancillary oxygenase during tetracycline biosynthesis. (Chembiochem. , 2009)
comment
>for C-terminal side

Blast 4th, id57%, 1e-113
Streptomyces rimosus_oxyE
OxyE

---
[PMID:18422316](2008)
完全に機能的なring Aを含む最初の中間体anhydrotetracycline (ATC)の生合成に必要な最小酵素セットの同定と再構築。

中間体6-methylpretetramid → ATC の変換にoxygenase候補OxyG, OxyE, or OxyRがあってもなくても、その産物特性と収量に影響なし。

---
[PMID:19472250](2009)
oxyE, oxyLの不活化とS. coelicolor CH999におけるoxyABCDJKNF + oxyE発現の産物解析により、OxyEは必須ではないが、より効率的な6-methylpretetramid C-4 hydroxylaseとして役立ち、oxytetracycline生合成において重要な役割をすることが示されている。

ここで実際に検出されているのは、いずれも4-hydroxy-6-methylpretetramidではなくその派生体だが、過去に4-hydroxy-6-methylpretetramidが中間体であることがわかっている。

[PMID:18422316](2008)のときにOxyEの機能を同定できなかったことについて、OxyLの強い発現と、競合するshunt glycosylation pathwaysを欠いたせいであると考察している。

close this sectionSequence

selected fasta
>putative biotin carboxylase/putative oxidoreductase [oxygenase]
MSTGDGMSTGGGTRAGDGPGGREGCLAVLIKAVLRTGVQALHPGYGFASENPDLAEVRED
HGSTSVGPSAPVIDRLGDKVSARALMAEAGLPLLPGGVEPAAGLEEARALAVETGYPLVI
KPVAGGGGRDTQVVRGPGEPAAKYRQPRGKAQGLFGDNRVYPECYRAAARHVEIQVFGDQ
LGNLVHLGEAALLGAKAAEYTGAGTFDFLVDDTGDFYSMEVNCRIQVEHPVTEVVTGVDL
VRERFRVAARLPLELSQSGVAPRGAAIECRQRHGPRPRPPADARPGRGVHRSGGTVRPSG
HGLLPRAPRIGGQRPVAGQGDHLGPRPRAGPGEDAPGTGRIPRERSRSAYEHPLPAPRAG
RSAFRRRHPHHVAHRGPHLTGAPRMTIDQTPRATGSTTDVCVIGGGPAGLTLALLLLRSG
VQVTLVERATSMSREYRGEILQPGGLALLDQLGVLAPAAARGGYWLDGFQLVERERVLLD
IAYDRLPAPYNRLLSVPQRHVLAELLDRCHGFDGFRYLDGHRLSALVEEDGAVRGAVAEG
RAGPHTVRAGWVVGADGRFSKTRRLAGIGADRQDVFAFDVLWFKLPQEEPPGRHVRVFRA
AGRPVLVYPSYPGTVQLGWTLPHKGYAEMATLGVETIRSEIARAVPAYADRLARHVHALS
DFTLLDVFAGRAREWVRDGLVLIGDSAHTHSPLGAQGINLALQDAALLHPVLVEALRDGD
FSAGRLDAYALPRSRDIDQVMKTQTMQAKAMLSQGRVARVVRPRLAGLVQRTPIGPKITR
HIALGNPAARVRSDLFAPG
selected fasta
>putative biotin carboxylase/putative oxidoreductase [oxygenase]
ATGAGCACCGGGGACGGCATGAGCACCGGGGGCGGGACGAGGGCGGGAGACGGCCCGGGC
GGGCGCGAGGGGTGTCTCGCGGTACTCATCAAGGCGGTCCTACGCACTGGGGTCCAGGCC
CTGCATCCCGGCTACGGATTCGCCTCCGAGAACCCCGACCTCGCCGAGGTCCGCGAGGAC
CACGGCAGCACTTCCGTCGGCCCGTCCGCGCCCGTCATCGACCGGCTGGGCGACAAGGTC
AGCGCTCGCGCGCTGATGGCCGAGGCCGGGCTGCCCCTGCTCCCCGGCGGTGTCGAACCG
GCGGCCGGCCTTGAGGAGGCCCGCGCCCTCGCCGTGGAGACCGGCTACCCGCTCGTCATC
AAACCGGTGGCCGGTGGGGGCGGCCGGGACACGCAGGTGGTGCGCGGCCCCGGCGAGCCG
GCGGCCAAGTACCGTCAGCCACGCGGCAAGGCGCAGGGCCTGTTCGGGGACAACCGGGTC
TATCCGGAGTGCTACCGCGCCGCCGCCCGGCACGTCGAGATCCAGGTGTTCGGTGACCAG
CTGGGCAATCTCGTCCACCTGGGGGAGGCGGCGCTGCTCGGGGCCAAGGCCGCCGAGTAC
ACAGGGGCGGGCACCTTCGACTTCCTGGTGGACGACACCGGCGACTTCTACTCTATGGAG
GTCAACTGCCGTATCCAGGTGGAACATCCCGTGACCGAGGTGGTCACCGGGGTGGACCTG
GTGCGCGAGCGGTTCCGGGTCGCGGCCCGTCTGCCGCTGGAACTCTCCCAGTCCGGCGTC
GCCCCGCGCGGTGCCGCGATCGAGTGCCGTCAACGCCATGGACCCCGCCCGCGACCTCCC
GCCGACGCACGGCCCGGTCGAGGAGTTCACCGCTCCGGCGGGACCGTTCGTCCTAGTGGA
CACGGACTGCTTCCCCGGGCACCGCGTATCGGCGGCCAACGACCCGTTGCCGGCCAAGGT
GATCACCTGGGCCCCCGACCGCGCGCAGGCCCGGGAGAGGATGCGCCGGGCACTGGACGC
ATTCCACGTGAACGGTCCCGGAGTGCGTACGAACATCCCCTTCCTGCGCCGCGTGCTGGA
CGCTCCGCGTTTCGCCGACGGCACCCACACCACGTCGCTCATCGCGGACCTCACCTCACA
GGAGCCCCTCGGATGACCATCGACCAGACCCCCCGCGCGACCGGCTCCACGACGGACGTC
TGTGTCATCGGCGGAGGCCCCGCCGGGCTGACCCTCGCCCTGCTCCTGCTCCGCTCCGGA
GTACAGGTCACCCTCGTCGAACGCGCGACCTCCATGTCGCGTGAGTACCGGGGCGAGATA
CTCCAGCCCGGCGGGCTGGCCCTGCTCGACCAGCTCGGCGTGCTGGCACCCGCCGCCGCG
CGCGGCGGGTACTGGCTGGACGGATTCCAGCTGGTGGAACGCGAGCGGGTGCTCCTCGAC
ATCGCCTACGACCGGCTGCCCGCGCCGTACAACCGCCTGCTCAGTGTTCCGCAGCGGCAC
GTACTGGCGGAACTGCTCGACCGCTGCCACGGGTTCGACGGCTTCCGCTATCTCGACGGA
CACCGGCTGAGCGCGCTCGTCGAGGAGGACGGAGCCGTCCGCGGTGCCGTCGCCGAGGGC
CGGGCCGGTCCCCACACCGTGCGTGCCGGATGGGTCGTCGGCGCCGACGGACGGTTCTCC
AAGACCCGGCGGCTCGCCGGGATCGGAGCCGATCGGCAGGACGTGTTCGCCTTCGACGTG
CTGTGGTTCAAACTGCCGCAGGAGGAACCACCCGGCCGGCACGTGCGCGTCTTCCGGGCC
GCGGGCCGGCCGGTGCTCGTCTACCCTTCGTACCCCGGCACCGTGCAGCTCGGCTGGACC
CTGCCGCACAAGGGGTACGCCGAGATGGCCACGCTCGGCGTCGAAACGATCAGGTCCGAG
ATCGCCCGCGCGGTCCCCGCGTACGCCGACCGGCTCGCCCGGCACGTCCACGCGCTCTCC
GACTTCACCCTGCTGGACGTCTTCGCCGGACGCGCGCGGGAGTGGGTGCGCGACGGCCTC
GTCCTGATCGGGGACAGCGCGCACACCCACAGCCCGCTCGGCGCCCAGGGCATCAACCTC
GCGCTTCAGGACGCCGCCCTGCTGCACCCCGTCCTCGTGGAGGCGTTGCGCGACGGCGAC
TTCTCGGCCGGACGGCTGGACGCCTACGCACTGCCGCGCTCCCGTGACATCGACCAGGTG
ATGAAGACACAGACGATGCAGGCCAAGGCGATGCTCTCGCAGGGCCGGGTGGCCCGGGTG
GTGCGTCCCCGGCTGGCCGGCCTCGTCCAGCGCACGCCCATCGGCCCGAAGATCACCCGG
CACATCGCGCTGGGCAACCCGGCCGCACGGGTGCGCTCCGACCTGTTCGCCCCCGGGTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
[398-741] 1.3e-44 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
[399-421] 5e-23 PR00420 [548-563] 5e-23 PR00420 [677-692] 5e-23 PR00420 [692-708] 5e-23 PR00420
PR00420   RNGMNOXGNASE
IPR005479 Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain (Domain)
[78-189] 4.5e-20 PF02786
PF02786   CPSase_L_D2
IPR005481 Carbamoyl-phosphate synthase, large subunit, N-terminal (Domain)
[29-73] 1.5e-07 PF00289
PF00289   CPSase_L_chain
IPR011761 ATP-grasp fold (Domain)
[83-300] 14.253 PS50975
PS50975   ATP_GRASP
IPR011764 Biotin carboxylation domain (Domain)
[1-799] 14.543 PS50979
PS50979   BC
IPR013815 ATP-grasp fold, subdomain 1 (Domain)
[93-163] 6.3e-13 G3DSA:3.30.1490.20
G3DSA:3.30.1490.20   no description
IPR013816 ATP-grasp fold, subdomain 2 (Domain)
[188-270] 8.2e-25 G3DSA:3.30.470.20
G3DSA:3.30.470.20   no description
IPR016185 Pre-ATP-grasp fold (Domain)
[29-76] 1.8e-14 SSF52440
SSF52440   PreATP-grasp domain
[29-92] 1.7e-15 G3DSA:3.40.50.20
G3DSA:3.40.50.20   no description
SignalP
[1-40] 0.346 Signal
Eukaryota   
[1-48] 0.284 Signal
Bacteria, Gram-negative   
TMHMM No significant hit
Chro_00060 Chro_00060   Chro_00080 Chro_00080
Page top