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Q93NW7

- Q93NW7_9ACTO

UniProt

Q93NW7 - Q93NW7_9ACTO

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Protein
Submitted name:

AmphB

Gene
amphB
Organism
Streptomyces nodosus
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei2858 – 28581NADPImported
Binding sitei2895 – 28951NADPImported
Binding sitei2924 – 29241NADP; via amide nitrogenImported
Binding sitei2929 – 29291NADP; via amide nitrogenImported

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi2756 – 27583NADPImported
Nucleotide bindingi2779 – 27802NADPImported
Nucleotide bindingi2807 – 28082NADPImported
Nucleotide bindingi2833 – 28353NADPImported

GO - Molecular functioni

  1. cofactor binding Source: InterPro
  2. nucleotide binding Source: UniProtKB-KW
  3. oxidoreductase activity Source: InterPro
  4. phosphopantetheine binding Source: InterPro
  5. transferase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotation

Keywords - Ligandi

NADPImported, Nucleotide-bindingImported

Names & Taxonomyi

Protein namesi
Submitted name:
AmphBImported
Gene namesi
Name:amphBImported
OrganismiStreptomyces nodosusImported
Taxonomic identifieri40318 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Keywords - PTMi

PhosphopantetheineUniRule annotation

Interactioni

Protein-protein interaction databases

DIPiDIP-59008N.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MJCX-ray1.48A/B2529-3003[»]
3MJEX-ray1.36A/B2529-3003[»]
3MJSX-ray1.40A/B2529-3003[»]
3MJTX-ray1.60A/B2529-3003[»]
3MJVX-ray1.46A/B2529-3003[»]
4DIFX-ray1.52A/B2529-3003[»]
ProteinModelPortaliQ93NW7.
SMRiQ93NW7. Positions 9-922, 1462-1552, 3015-3105.

Miscellaneous databases

EvolutionaryTraceiQ93NW7.

Family & Domainsi

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.720. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR002198. DH_sc/Rdtase_SDR.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 2 hits.
PF00106. adh_short. 1 hit.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF08659. KR. 1 hit.
PF00550. PP-binding. 2 hits.
[Graphical view]
SMARTiSM00827. PKS_AT. 2 hits.
SM00822. PKS_KR. 2 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 2 hits.
SSF52151. SSF52151. 4 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 2 hits.
PROSITEiPS50075. ACP_DOMAIN. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93NW7-1 [UniParc]FASTAAdd to Basket

« Hide

MPEPQQNQQE KVVDYLRRVT NDLRRARRRI GELESRDNEP VAIVGMSCRL     50
PGGVSSPESL WELVESGGDA ISGFPADRGW DIEALTGKGE GSSSTHEGGF 100
LYEATDFDAG FFGISPREAT AMDPQQRLLL EVSWEALERA GIAPTSLRSS 150
ATGVFVGSYH WGAPSADTAT ELHGHALTGT AASVLSGRLS YVYGLEGPAV 200
TVDTACSSSL VALHMAAQSL RNGESSLALV GGVTILAEPS VFVEFSAQGG 250
LAQDGRCKAF SDSADGTGWS EGAAVLVVER LSDARRAGHR VLAVVRGSAV 300
NQDGASNGLT APNGPSQQRV IRQALANAGL RPGDVDAVEA HGTGTPLGDP 350
IEAQALIATY GSDRDPQQPL LLGSVKSNIG HTQSAAGVAG LVKMVMAMHN 400
GTLPRTLHLT EPSTHVDWSL GAVRLLTEET AWPETGRVRR AAVSSFGISG 450
TNAHAVLEQA PVPAEDAEDA GTEDAPQQPA TVPGALPWLL SAHSGQALCD 500
QAAALVTRLD ADPEPRPQDI GQGLLTSRAL LERRAVVVGT GRDELLTGSR 550
ALAEGQSWNG LAEGTADVDG RTVFVFPGQG SQWVGMGARL LDESPVFAER 600
IAECAAALAE FTDWDLLDVL RGAEGAPTLE RVDVVQPASF AVMVSLAAVW 650
RAQGVEPDAV VGHSQGEIAA AVVSGALSLR DGARVVALRS QAIGRTLAGR 700
GGMMSVALPV ADVEARLEAF GGRVSVAAEN GPRSCVVSGE PGALDELSEL 750
LTAEGVRVRR VPVDYASHSH HVEDLHDEIL QLLAEVAPKA SEVPLFSTVT 800
GDWLDTTVMD AGYWFRSLRG RVLFADAIRG LLDTEHRAFI EVSSHPVLAM 850
SVQDMIDDAG VVGVASGTLR RDNGGLDRFL LSAAQVFVRG VQVDWAPLFE 900
GTGATRVDLP TYAFQHERYW NDRAVVDRSA SAPMDAEFWA AVEQADVSAL 950
TEALGTDEES VAAILPGLAS WRRTRGERST VDSWRYRVVW EPLAQIPRAT 1000
LDGTWLLVSA GGVDDDVAEV LEAGGAEVRR LVLDETCTDP AVLREHLTDT 1050
DGLTGIVSVL ADAEEGCVRH PGLTLGLALS VSLAQALGEA DVTAPLWFLT 1100
CGAFSTGPSD TVTRPLQSQI AGLGWTVAVE HPHRWGGGVD LPEALDARAA 1150
QRLVAALAGA LGDDDQLAVR PAGVLARRIV RASGDTRRKA RSWKPRGTTL 1200
VTGGSGTLAP GLARHLAAQG AEHLVLLSRR GADAPGAAEL AAELQAAGTE 1250
VRFAACDITD PDAVAALLAD LKAEGRTVRT VVHTAAVIEL AALADTTVDA 1300
FADVVHAKVT GARILDELLD DEELDDFVLY SSTAGMWGSG VHAAYVAGNA 1350
YLSALAEQRR ARGARATSIH WGKWPDDLER ELADPHQIRR SGLEYLDPEL 1400
AMTALTRVME DDETVIGLMD IDWGTYHDVF TAGRPSHLFD RIPEVARLLA 1450
DRAAPAATAV ATSGLAARLQ GVSAAEQDRI VLSVVREETA AVLGHASAET 1500
VPERRAFRDI GFDSVTAVDL RNRLVAATGL TLPSTMVFDH PNAVALATFL 1550
KATALGTTGT AGDRPTAAVT AGADDDLIVI VGMSCRFPGG ANTPEELLRL 1600
ALDGADVISE FPADRGWDAH GLYDPDPDRQ GRTYSVHGGF LHEAAGFDAG 1650
FFGISPREAL AMDPQQRLLL ETSWEVLERA GIDPESLHST ATGAFFGASY 1700
QDYSSSVQNG TEGAEVHMMT GTAASVLSGR ISYLLGLEGP AVTVDTACSS 1750
SLVAMHLACQ SLRSGESSLA LAGGAAVMAT PHAFIGFSRQ RALAENGRCK 1800
PFAEGADGMT LAEGVGVVLL EKLSDARRNG HRVLAVVRGS ALNQDGASNG 1850
LTAPNGLSQQ RVIRQALANA GLGTADIDVV EAHGTGTKLG DPIEAGALLA 1900
TYGQGRDGGQ PLLLGSVKSN IGHTQAAAGV AGVIKMVMAM HAGELPGTLH 1950
IDEPSSHVDW TSGAVTLLRE RTEWPAVGDR PRRAGISSFG ISGTNAHLLL 2000
EQAPPAEEPA EEPAGDIEGA PLVPWLLSAR SAQALREQAS RLLTATTGTD 2050
VTVEPARVGH ALATTRTAFD HRAVVLGSRP EDFTRGLEAV VSSASAPGVV 2100
TGTAGPDSTG PVFVYPGQGS QWWGMGRELL AGSEVFRTAV DDCAAALAPY 2150
TDWSLHEVLA GEGDPELLER VDVVQPALFS MMVALTALWR SHGVEPAAVV 2200
GHSQGEIAAA HVAGALSLED AALVVALRSQ ALPQLSGLGG MMSVSAPAAR 2250
VTELLQPWGE ALSIAAVNGP SSVIVSGDAD ALDELLETCR EQNVRARKVS 2300
VDYASHGRHV EAVRDELARV LAPVSPRTPE VPFYSTVTGA RLDEAAFDGT 2350
YWYTNLRQTV LMEDATRALI ASGHRVFVEI SPHPVLAAPI QETQESVQEE 2400
LTETGAVLGT LRRDDGDRRR FLTSLAEAHT HGIAVDWTTA FDRPAYAAVD 2450
LPTYPFQRQD FWPEPKTAAP AGTADASDAA FWELVQNQDL DALAGELGIP 2500
ADDGAARLGD VLPALSAWRT RSLTRSRADA LRYHIEWNRV AEPGTARPAG 2550
RLLAVISPDH AGAPWVTAVL DALGPDTVRF EAKGTDRAAW AAQLAQLRED 2600
EGEFHAVVSL LAAAEALHTD HGSVPLGLAQ TLLLAQALGD AGLTAPLWCL 2650
TRGGVAAGRG DVLSSPVQGA LWGLGRVIGL EHPDRWGGLI DLPETVDTRA 2700
AARLTGLLAD AGGEDQLAIR GSGVLARRLA HAAPAVPGSG KRPPVHGSVL 2750
VTGGTGGIGG RVARRLAEQG AAHLVLTSRR GADAPGAAEL RAELEQLGVR 2800
VTIAACDAAD REALAALLAE LPEDAPLTAV FHSAGVAHDD APVADLTLGQ 2850
LDALMRAKLT AARHLHELTA DLDLDAFVLF SSGAAVWGSG GQPGYAAANA 2900
YLDALAEHRR SLGLTASSVA WGTWGEVGMA TDPEVHDRLV RQGVLAMEPE 2950
HALGALDQML ENDDTAAAIT LMDWEMFAPA FTANRPSALL STVPEAVSAL 3000
SDEGPADGGA DAAVPPLRAR LDGLPTAERA RALVEAVRAE ASATLGHDSP 3050
DAVPASRAFR DVGFDSVTAV ELRNRLRAAL GLPLPAALVF DYPTPTALAQ 3100
HIGSLLYGTA PDEADTGRAD DPDARIREAL ATVPIGRLRK AGLLDMVLKL 3150
AESDDTEDSA TATDDAADAL DLDDMDAEAL LRLAAENSAN 3190
Length:3,190
Mass (Da):334,066
Last modified:December 1, 2001 - v1
Checksum:iEC005DABF792D89B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF357202 Genomic DNA. Translation: AAK73513.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF357202 Genomic DNA. Translation: AAK73513.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MJC X-ray 1.48 A/B 2529-3003 [» ]
3MJE X-ray 1.36 A/B 2529-3003 [» ]
3MJS X-ray 1.40 A/B 2529-3003 [» ]
3MJT X-ray 1.60 A/B 2529-3003 [» ]
3MJV X-ray 1.46 A/B 2529-3003 [» ]
4DIF X-ray 1.52 A/B 2529-3003 [» ]
ProteinModelPortali Q93NW7.
SMRi Q93NW7. Positions 9-922, 1462-1552, 3015-3105.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59008N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q93NW7.

Family and domain databases

Gene3Di 1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.720. 2 hits.
InterProi IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR002198. DH_sc/Rdtase_SDR.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 2 hits.
PF00106. adh_short. 1 hit.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF08659. KR. 1 hit.
PF00550. PP-binding. 2 hits.
[Graphical view ]
SMARTi SM00827. PKS_AT. 2 hits.
SM00822. PKS_KR. 2 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
[Graphical view ]
SUPFAMi SSF47336. SSF47336. 2 hits.
SSF52151. SSF52151. 4 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 2 hits.
PROSITEi PS50075. ACP_DOMAIN. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Amphotericin biosynthesis in Streptomyces nodosus: deductions from analysis of polyketide synthase and late genes."
    Caffrey P., Lynch S., Flood E., Finnan S., Oliynyk M.
    Chem. Biol. 8:713-723(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Biosynthesis of amphotericin derivatives lacking exocyclic carboxyl groups."
    Carmody M., Murphy B., Byrne B., Power P., Rai D., Rawlings B., Caffrey P.
    J. Biol. Chem. 280:34420-34426(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Structural and functional analysis of A-type ketoreductases from the amphotericin modular polyketide synthase."
    Zheng J., Taylor C.A., Piasecki S.K., Keatinge-Clay A.T.
    Structure 18:913-922(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 2529-3003 IN COMPLEX WITH NADP.
  4. "Structure and mutagenesis of A2-type ketoreductase from modular polyketide synthase reveals insights into stereospecificity."
    Zheng J., Keatinge-Clay A.T.
    Submitted (JAN-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 2529-3003 IN COMPLEX WITH NADP.

Entry informationi

Entry nameiQ93NW7_9ACTO
AccessioniPrimary (citable) accession number: Q93NW7
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

Similar proteinsi