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Protein
Submitted name:

Type I polyketide synthase PikAIV

Gene

pikAIV

Organism
Streptomyces venezuelae
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18414.

Protein family/group databases

ESTHERistrve-PIKAIV. Thioesterase.

Names & Taxonomyi

Protein namesi
Submitted name:
Type I polyketide synthase PikAIVImported
Gene namesi
Name:pikAIVImported
OrganismiStreptomyces venezuelaeImported
Taxonomic identifieri54571 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MN6X-ray2.20A/B1049-1346[»]
1MNAX-ray1.80A/B1049-1346[»]
1MNQX-ray2.20A/B1049-1346[»]
2H7XX-ray1.85A/B1049-1346[»]
2H7YX-ray2.10A/B1049-1346[»]
2HFJX-ray1.95A/B1049-1346[»]
2HFKX-ray1.79A/B1049-1346[»]
3F5HX-ray1.75A/B1-37[»]
ProteinModelPortaliQ9ZGI2.
SMRiQ9ZGI2. Positions 34-906, 1057-1339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZGI2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini944 – 101774Acyl carrierInterPro annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili5 – 2925Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

KOiK16003.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53474. SSF53474. 2 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZGI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSNEQLVD ALRASLKENE ELRKESRRRA DRRQEPMAIV GMSCRFAGGI
60 70 80 90 100
RSPEDLWDAV AAGKDLVSEV PEERGWDIDS LYDPVPGRKG TTYVRNAAFL
110 120 130 140 150
DDAAGFDAAF FGISPREALA MDPQQRQLLE ASWEVFERAG IDPASVRGTD
160 170 180 190 200
VGVYVGCGYQ DYAPDIRVAP EGTGGYVVTG NSSAVASGRI AYSLGLEGPA
210 220 230 240 250
VTVDTACSSS LVALHLALKG LRNGDCSTAL VGGVAVLATP GAFIEFSSQQ
260 270 280 290 300
AMAADGRTKG FASAADGLAW GEGVAVLLLE RLSDARRKGH RVLAVVRGSA
310 320 330 340 350
INQDGASNGL TAPHGPSQQH LIRQALADAR LTSSDVDVVE GHGTGTRLGD
360 370 380 390 400
PIEAQALLAT YGQGRAPGQP LRLGTLKSNI GHTQAASGVA GVIKMVQALR
410 420 430 440 450
HGVLPKTLHV DEPTDQVDWS AGSVELLTEA VDWPERPGRL RRAGVSAFGV
460 470 480 490 500
GGTNAHVVLE EAPAVEESPA VEPPAGGGVV PWPVSAKTSA ALDAQIGQLA
510 520 530 540 550
AYAEDRTDVD PAVAARALVD SRTAMEHRAV AVGDSREALR DALRMPEGLV
560 570 580 590 600
RGTVTDPGRV AFVFPGQGTQ WAGMGAELLD SSPEFAAAMA ECETALSPYV
610 620 630 640 650
DWSLEAVVRQ APSAPTLDRV DVVQPVTFAV MVSLAKVWQH HGITPEAVIG
660 670 680 690 700
HSQGEIAAAY VAGALTLDDA ARVVTLRSKS IAAHLAGKGG MISLALSEEA
710 720 730 740 750
TRQRIENLHG LSIAAVNGPT ATVVSGDPTQ IQELAQACEA DGIRARIIPV
760 770 780 790 800
DYASHSAHVE TIENELADVL AGLSPQTPQV PFFSTLEGTW ITEPALDGGY
810 820 830 840 850
WYRNLRHRVG FAPAVETLAT DEGFTHFIEV SAHPVLTMTL PDKVTGLATL
860 870 880 890 900
RREDGGQHRL TTSLAEAWAN GLALDWASLL PATGALSPAV PDLPTYAFQH
910 920 930 940 950
RSYWISPAGP GEAPAHTASG REAVAETGLA WGPGAEDLDE EGRRSAVLAM
960 970 980 990 1000
VMRQAASVLR CDSPEEVPVD RPLREIGFDS LTAVDFRNRV NRLTGLQLPP
1010 1020 1030 1040 1050
TVVFQHPTPV ALAERISDEL AERNWAVAEP SDHEQAEEEK AAAPAGARSG
1060 1070 1080 1090 1100
ADTGAGAGMF RALFRQAVED DRYGEFLDVL AEASAFRPQF ASPEACSERL
1110 1120 1130 1140 1150
DPVLLAGGPT DRAEGRAVLV GCTGTAANGG PHEFLRLSTS FQEERDFLAV
1160 1170 1180 1190 1200
PLPGYGTGTG TGTALLPADL DTALDAQARA ILRAAGDAPV VLLGHSGGAL
1210 1220 1230 1240 1250
LAHELAFRLE RAHGAPPAGI VLVDPYPPGH QEPIEVWSRQ LGEGLFAGEL
1260 1270 1280 1290 1300
EPMSDARLLA MGRYARFLAG PRPGRSSAPV LLVRASEPLG DWQEERGDWR
1310 1320 1330 1340
AHWDLPHTVA DVPGDHFTMM RDHAPAVAEA VLSWLDAIEG IEGAGK
Length:1,346
Mass (Da):141,914
Last modified:May 1, 1999 - v1
Checksum:i3E149C8044FBE5F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079138 Genomic DNA. Translation: AAC69332.1.
PIRiT17412.

Genome annotation databases

KEGGiag:AAC69332.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079138 Genomic DNA. Translation: AAC69332.1.
PIRiT17412.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MN6X-ray2.20A/B1049-1346[»]
1MNAX-ray1.80A/B1049-1346[»]
1MNQX-ray2.20A/B1049-1346[»]
2H7XX-ray1.85A/B1049-1346[»]
2H7YX-ray2.10A/B1049-1346[»]
2HFJX-ray1.95A/B1049-1346[»]
2HFKX-ray1.79A/B1049-1346[»]
3F5HX-ray1.75A/B1-37[»]
ProteinModelPortaliQ9ZGI2.
SMRiQ9ZGI2. Positions 34-906, 1057-1339.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERistrve-PIKAIV. Thioesterase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC69332.

Phylogenomic databases

KOiK16003.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18414.

Miscellaneous databases

EvolutionaryTraceiQ9ZGI2.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53474. SSF53474. 2 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity."
    Xue Y., Zhao L., Liu H.w., Sherman D.H.
    Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC15439Imported.
  2. "Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases."
    Tsai S.C., Lu H., Cane D.E., Khosla C., Stroud R.M.
    Biochemistry 41:12598-12606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1049-1346.
  3. "Structural and mechanistic insights into polyketide macrolactonization from polyketide-based affinity labels."
    Giraldes J.W., Akey D.L., Kittendorf J.D., Sherman D.H., Smith J.L., Fecik R.A.
    Nat. Chem. Biol. 2:531-536(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1049-1346.
  4. "Structural basis for macrolactonization by the pikromycin thioesterase."
    Akey D.L., Kittendorf J.D., Giraldes J.W., Fecik R.A., Sherman D.H., Smith J.L.
    Nat. Chem. Biol. 2:537-542(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 1049-1346.
  5. "Structural basis for binding specificity between subclasses of modular polyketide synthase docking domains."
    Buchholz T.J., Geders T.W., Bartley F.E., Reynolds K.A., Smith J.L., Sherman D.H.
    ACS Chem. Biol. 4:41-52(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-37.

Entry informationi

Entry nameiQ9ZGI2_STRVZ
AccessioniPrimary (citable) accession number: Q9ZGI2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.