Nanch_00170 : CDS information

Location

Organism	Streptomyces nanchangensis
Strain	NS3226
Entry name	Nanchangmycin
Contig	AF521085
Start / Stop / Direction	68,860 / 70,164 / + [in whole cluster] 68,860 / 70,164 / + [in contig]
Location	68860..70164 [in whole cluster] 68860..70164 [in contig]
Type	CDS
Length	1,305 bp (434 aa)

Annotation

Category	2.3 modification addition of sugar moiety
Product	putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase
Product (GenBank)	NanG3
Gene
Gene (GenBank)	nanG3
EC number
Keyword	4-O-methyl-L-rhodinose
Note
Note (GenBank)	putative NDP-D-glucose-3,4-dehydratase
Reference	ACC Q7WTE6 PmId [12770825] A complete gene cluster from Streptomyces nanchangensis NS3226 encoding biosynthesis of the polyether ionophore nanchangmycin. (Chem Biol. , 2003) comment Nanchangmycin生合成のためのcomplete gene clusterの報告。（complete clusterと言っているが、同定されたclusterがNanchangmycin生合成に十分かは確認されていない。）配列解析からの機能予測。 NanG3: NDP-D-glucose-3,4-dehydratase and perosamine synthase 4-O-methyl-L-rhodinose生合成経路を提唱しているFig. 4では、 dTDP-4-keto-6-deoxy-D-Glu ↓dehydratase dTDP-4-keto-2,6-dideoxy-D-Glu に機能割り当てされている。
Related Reference	ACC Q9L4S6 NITE Urd_00240 PmId [11094336] The NDP-sugar co-substrate concentration and the enzyme expression level influence the substrate specificity of glycosyltransferases: cloning and characterization of deoxysugar biosynthetic genes of the urdamycin biosynthetic gene cluster. (Chem Biol. , 2000) [17434221] Surprising production of a new urdamycin derivative by S. fradiae Delta urdQ/R. (J Biotechnol. , 2007) comment 4th(Q9L4S6) 79%, 0.0 Streptomyces fradiae_urdQ NDP-hexose 3,4-dehydratase UrdQ [Urd_00240]putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase --- [PMID: 11094336](2000) urdZ3, urdQ and urdZ1をそれぞれ不活化するとL-rhodinoseを産生できない株となり、主にurdamycinone B (D-olivoseあり、L-rhodinoseなし)を蓄積。各genesで相補され、urdamycin A産生回復。よってこれらのgenesはNDP-L-rhodinose生合成にのみ関与する。 urdamycin deoxysugar(NDP-D-olivose, NDP-L-rhodinose)生合成経路のFigあり。 UrdQ = NDP-4-keto-2,6-dideoxy-D-glucose → NDP-D-cinerulose この機能的割り当てを確認するにはさらなる研究が必要。 --- [PMID: 17434221](2007) urdQ/R double mutantの相補実験あり。 S. cyanogenus S136に由来するlandomycin生合成gene clusterの dTDP-hexose-3,4-dehydrataseをコードするlanQと、 dTDP-hexose-4-ketoreductaseをコードするlanRでの相補は、 urdamycin A and urdamycin Bの産生をもたらした。ただ、lanQ,lanR自体が機能確認されていないようなので微妙。
Related Reference	ACC Q9ALN8 NITE Spino_00050 PmId [17076492] Characterization of SpnQ from the spinosyn biosynthetic pathway of Saccharopolyspora spinosa: mechanistic and evolutionary implications for C-3 deoxygenation in deoxysugar biosynthesis. (J Am Chem Soc. , 2006) [18345667] In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa. (J Am Chem Soc. , 2008) comment 20th(Q9ALN8) 71%, 1e-164 Saccharopolyspora spinosa_spnQ Probable NDP-hexose-3,4-dehydratase [Spino_00050]pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase forosamine生合成におけるC-3 deoxygenationに関与したPMP-dependent 3-dehydrataseであるという報告あり。 --- [PMID: 17076492](2006) SpnQをクローニング、過剰発現、精製して、"ColD-like" conditions と "E1-like" conditionsの両方で触媒活性をテスト。 E3のような特異的reductaseを必要とせず、一般的なferredoxin/ferredoxin reductase またはflavodoxin/flavodoxin reductaseと効率的に働く。 --- [PMID: 18345667](2008) dTDP-D-forosamine形成に関連する5つの酵素SpnO, N, Q, R, and Sの生化学的機能解明。使用している株はNRRL 18537. SpnQのsteady-state kinetic parameters、基質特異性を調査。

Sequence

>putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [NanG3]
MSERVARILDEVRKYHQDSQEGRGFIPGVTEIWPSGAVLDEDDRVALVQAALEMRIAAGK
LSRKFESAFARRMKRRKAHLTNSGSSANLLAISALTSHLLGERRLRPGDEVITVAASFPT
TVNPILQNGLVPVYVDVELGTYNATAERVAEAIGPRTRAIMMAHTLGNPFQATEMARLAQ
DHDLILIEDSCDAVGSTYDGRPAGTFGDLTTVSFYPAHHLTMGEGGCVLTSNLVLARIVE
SLRDWGRDCWCEPGESDTCRKRFGYQMGTLPAGYDHKYIFSHIGYNLKSTDLQAALGLTQ
LDKLDAFCSARRSNWRRLREGLDGLPWLILPEATPRSDPSWFGFVLTVDPRAPFSRAELV
DFLESRKIGTRRLFAGNLTRHPAHAEAPHRVCGDLANSDTVTEHTFWVGVYPGLTEEMID
FMVSSITEFIGSHR

>putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [NanG3]
ATGAGCGAACGGGTCGCGCGCATCCTCGACGAGGTGCGCAAGTACCACCAGGACAGCCAG
GAGGGGCGTGGCTTCATCCCCGGGGTCACCGAGATCTGGCCCTCGGGCGCGGTGCTCGAC
GAGGACGACCGGGTCGCGCTGGTGCAGGCCGCGCTGGAGATGCGGATCGCCGCGGGCAAG
CTCTCCCGGAAGTTCGAGTCGGCCTTCGCGCGCCGGATGAAGCGCCGCAAGGCACACCTG
ACGAACTCCGGGTCGTCCGCGAACCTCCTCGCGATCTCCGCGCTGACCTCCCACCTGCTG
GGCGAGCGCCGGCTGCGCCCGGGCGACGAGGTCATCACGGTGGCGGCGAGCTTCCCCACC
ACCGTCAACCCGATCCTGCAGAACGGGCTTGTCCCGGTCTATGTGGACGTCGAGTTGGGG
ACGTACAACGCCACGGCCGAGCGGGTGGCGGAGGCGATCGGGCCGCGCACCCGGGCCATC
ATGATGGCGCACACGCTGGGCAACCCCTTCCAGGCCACGGAGATGGCCCGGCTGGCGCAG
GACCACGACCTGATTTTGATCGAGGACAGCTGCGACGCCGTGGGCTCCACCTATGACGGG
CGGCCGGCCGGGACGTTCGGCGATCTGACGACCGTCAGCTTCTACCCCGCGCACCATCTG
ACCATGGGTGAGGGCGGCTGCGTGCTGACCTCGAACCTGGTCCTGGCGCGGATCGTGGAG
TCGCTGCGGGACTGGGGCCGGGACTGCTGGTGCGAGCCGGGCGAGAGCGACACATGCCGC
AAGCGGTTCGGGTACCAGATGGGCACGCTGCCGGCCGGCTACGACCACAAGTACATCTTC
TCCCACATCGGGTACAACCTGAAGTCGACCGACCTCCAGGCGGCGCTCGGGCTGACCCAG
CTCGACAAGCTCGACGCGTTCTGCTCGGCCCGTCGGAGCAACTGGCGGCGGCTGCGCGAA
GGGCTGGACGGGCTGCCGTGGCTGATCCTGCCGGAGGCGACGCCGCGCTCCGATCCGAGC
TGGTTCGGGTTCGTCCTGACCGTCGATCCGCGGGCCCCGTTCAGCCGCGCCGAGCTGGTC
GACTTCCTGGAGTCCCGCAAGATCGGCACACGTCGGCTGTTCGCCGGGAACCTGACGCGC
CATCCCGCGCATGCCGAAGCGCCACACCGGGTGTGCGGCGATCTGGCCAACAGCGACACC
GTCACCGAGCACACGTTCTGGGTCGGCGTCTATCCAGGGCTGACCGAGGAGATGATCGAC
TTCATGGTCTCCTCCATCACCGAGTTCATCGGGAGCCACCGGTGA

Feature

BLASTP Database:UniProtKB:2011_09	show BLAST table
InterPro Database:interpro:38.0	IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase (Family) PF01041 DegT_DnrJ_EryC1 PIRSF000390 PLP_StrS IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1 (Domain) G3DSA:3.40.640.10 PyrdxlP-dep_Trfase_major_sub1 IPR015422 Pyridoxal phosphate-dependent transferase, major region, subdomain 2 (Domain) G3DSA:3.90.1150.10 PyrdxlP-dep_Trfase_major_sub2 IPR015424 Pyridoxal phosphate-dependent transferase, major domain (Domain) SSF53383 PyrdxlP-dep_Trfase_major
SignalP	No significant hit
TMHMM	No significant hit

Nanch_00160 Nanch_00180