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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: 1 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:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MPEPQQNQQE KVVDYLRRVT NDLRRARRRI GELESRDNEP VAIVGMSCRL
60 70 80 90 100
PGGVSSPESL WELVESGGDA ISGFPADRGW DIEALTGKGE GSSSTHEGGF
110 120 130 140 150
LYEATDFDAG FFGISPREAT AMDPQQRLLL EVSWEALERA GIAPTSLRSS
160 170 180 190 200
ATGVFVGSYH WGAPSADTAT ELHGHALTGT AASVLSGRLS YVYGLEGPAV
210 220 230 240 250
TVDTACSSSL VALHMAAQSL RNGESSLALV GGVTILAEPS VFVEFSAQGG
260 270 280 290 300
LAQDGRCKAF SDSADGTGWS EGAAVLVVER LSDARRAGHR VLAVVRGSAV
310 320 330 340 350
NQDGASNGLT APNGPSQQRV IRQALANAGL RPGDVDAVEA HGTGTPLGDP
360 370 380 390 400
IEAQALIATY GSDRDPQQPL LLGSVKSNIG HTQSAAGVAG LVKMVMAMHN
410 420 430 440 450
GTLPRTLHLT EPSTHVDWSL GAVRLLTEET AWPETGRVRR AAVSSFGISG
460 470 480 490 500
TNAHAVLEQA PVPAEDAEDA GTEDAPQQPA TVPGALPWLL SAHSGQALCD
510 520 530 540 550
QAAALVTRLD ADPEPRPQDI GQGLLTSRAL LERRAVVVGT GRDELLTGSR
560 570 580 590 600
ALAEGQSWNG LAEGTADVDG RTVFVFPGQG SQWVGMGARL LDESPVFAER
610 620 630 640 650
IAECAAALAE FTDWDLLDVL RGAEGAPTLE RVDVVQPASF AVMVSLAAVW
660 670 680 690 700
RAQGVEPDAV VGHSQGEIAA AVVSGALSLR DGARVVALRS QAIGRTLAGR
710 720 730 740 750
GGMMSVALPV ADVEARLEAF GGRVSVAAEN GPRSCVVSGE PGALDELSEL
760 770 780 790 800
LTAEGVRVRR VPVDYASHSH HVEDLHDEIL QLLAEVAPKA SEVPLFSTVT
810 820 830 840 850
GDWLDTTVMD AGYWFRSLRG RVLFADAIRG LLDTEHRAFI EVSSHPVLAM
860 870 880 890 900
SVQDMIDDAG VVGVASGTLR RDNGGLDRFL LSAAQVFVRG VQVDWAPLFE
910 920 930 940 950
GTGATRVDLP TYAFQHERYW NDRAVVDRSA SAPMDAEFWA AVEQADVSAL
960 970 980 990 1000
TEALGTDEES VAAILPGLAS WRRTRGERST VDSWRYRVVW EPLAQIPRAT
1010 1020 1030 1040 1050
LDGTWLLVSA GGVDDDVAEV LEAGGAEVRR LVLDETCTDP AVLREHLTDT
1060 1070 1080 1090 1100
DGLTGIVSVL ADAEEGCVRH PGLTLGLALS VSLAQALGEA DVTAPLWFLT
1110 1120 1130 1140 1150
CGAFSTGPSD TVTRPLQSQI AGLGWTVAVE HPHRWGGGVD LPEALDARAA
1160 1170 1180 1190 1200
QRLVAALAGA LGDDDQLAVR PAGVLARRIV RASGDTRRKA RSWKPRGTTL
1210 1220 1230 1240 1250
VTGGSGTLAP GLARHLAAQG AEHLVLLSRR GADAPGAAEL AAELQAAGTE
1260 1270 1280 1290 1300
VRFAACDITD PDAVAALLAD LKAEGRTVRT VVHTAAVIEL AALADTTVDA
1310 1320 1330 1340 1350
FADVVHAKVT GARILDELLD DEELDDFVLY SSTAGMWGSG VHAAYVAGNA
1360 1370 1380 1390 1400
YLSALAEQRR ARGARATSIH WGKWPDDLER ELADPHQIRR SGLEYLDPEL
1410 1420 1430 1440 1450
AMTALTRVME DDETVIGLMD IDWGTYHDVF TAGRPSHLFD RIPEVARLLA
1460 1470 1480 1490 1500
DRAAPAATAV ATSGLAARLQ GVSAAEQDRI VLSVVREETA AVLGHASAET
1510 1520 1530 1540 1550
VPERRAFRDI GFDSVTAVDL RNRLVAATGL TLPSTMVFDH PNAVALATFL
1560 1570 1580 1590 1600
KATALGTTGT AGDRPTAAVT AGADDDLIVI VGMSCRFPGG ANTPEELLRL
1610 1620 1630 1640 1650
ALDGADVISE FPADRGWDAH GLYDPDPDRQ GRTYSVHGGF LHEAAGFDAG
1660 1670 1680 1690 1700
FFGISPREAL AMDPQQRLLL ETSWEVLERA GIDPESLHST ATGAFFGASY
1710 1720 1730 1740 1750
QDYSSSVQNG TEGAEVHMMT GTAASVLSGR ISYLLGLEGP AVTVDTACSS
1760 1770 1780 1790 1800
SLVAMHLACQ SLRSGESSLA LAGGAAVMAT PHAFIGFSRQ RALAENGRCK
1810 1820 1830 1840 1850
PFAEGADGMT LAEGVGVVLL EKLSDARRNG HRVLAVVRGS ALNQDGASNG
1860 1870 1880 1890 1900
LTAPNGLSQQ RVIRQALANA GLGTADIDVV EAHGTGTKLG DPIEAGALLA
1910 1920 1930 1940 1950
TYGQGRDGGQ PLLLGSVKSN IGHTQAAAGV AGVIKMVMAM HAGELPGTLH
1960 1970 1980 1990 2000
IDEPSSHVDW TSGAVTLLRE RTEWPAVGDR PRRAGISSFG ISGTNAHLLL
2010 2020 2030 2040 2050
EQAPPAEEPA EEPAGDIEGA PLVPWLLSAR SAQALREQAS RLLTATTGTD
2060 2070 2080 2090 2100
VTVEPARVGH ALATTRTAFD HRAVVLGSRP EDFTRGLEAV VSSASAPGVV
2110 2120 2130 2140 2150
TGTAGPDSTG PVFVYPGQGS QWWGMGRELL AGSEVFRTAV DDCAAALAPY
2160 2170 2180 2190 2200
TDWSLHEVLA GEGDPELLER VDVVQPALFS MMVALTALWR SHGVEPAAVV
2210 2220 2230 2240 2250
GHSQGEIAAA HVAGALSLED AALVVALRSQ ALPQLSGLGG MMSVSAPAAR
2260 2270 2280 2290 2300
VTELLQPWGE ALSIAAVNGP SSVIVSGDAD ALDELLETCR EQNVRARKVS
2310 2320 2330 2340 2350
VDYASHGRHV EAVRDELARV LAPVSPRTPE VPFYSTVTGA RLDEAAFDGT
2360 2370 2380 2390 2400
YWYTNLRQTV LMEDATRALI ASGHRVFVEI SPHPVLAAPI QETQESVQEE
2410 2420 2430 2440 2450
LTETGAVLGT LRRDDGDRRR FLTSLAEAHT HGIAVDWTTA FDRPAYAAVD
2460 2470 2480 2490 2500
LPTYPFQRQD FWPEPKTAAP AGTADASDAA FWELVQNQDL DALAGELGIP
2510 2520 2530 2540 2550
ADDGAARLGD VLPALSAWRT RSLTRSRADA LRYHIEWNRV AEPGTARPAG
2560 2570 2580 2590 2600
RLLAVISPDH AGAPWVTAVL DALGPDTVRF EAKGTDRAAW AAQLAQLRED
2610 2620 2630 2640 2650
EGEFHAVVSL LAAAEALHTD HGSVPLGLAQ TLLLAQALGD AGLTAPLWCL
2660 2670 2680 2690 2700
TRGGVAAGRG DVLSSPVQGA LWGLGRVIGL EHPDRWGGLI DLPETVDTRA
2710 2720 2730 2740 2750
AARLTGLLAD AGGEDQLAIR GSGVLARRLA HAAPAVPGSG KRPPVHGSVL
2760 2770 2780 2790 2800
VTGGTGGIGG RVARRLAEQG AAHLVLTSRR GADAPGAAEL RAELEQLGVR
2810 2820 2830 2840 2850
VTIAACDAAD REALAALLAE LPEDAPLTAV FHSAGVAHDD APVADLTLGQ
2860 2870 2880 2890 2900
LDALMRAKLT AARHLHELTA DLDLDAFVLF SSGAAVWGSG GQPGYAAANA
2910 2920 2930 2940 2950
YLDALAEHRR SLGLTASSVA WGTWGEVGMA TDPEVHDRLV RQGVLAMEPE
2960 2970 2980 2990 3000
HALGALDQML ENDDTAAAIT LMDWEMFAPA FTANRPSALL STVPEAVSAL
3010 3020 3030 3040 3050
SDEGPADGGA DAAVPPLRAR LDGLPTAERA RALVEAVRAE ASATLGHDSP
3060 3070 3080 3090 3100
DAVPASRAFR DVGFDSVTAV ELRNRLRAAL GLPLPAALVF DYPTPTALAQ
3110 3120 3130 3140 3150
HIGSLLYGTA PDEADTGRAD DPDARIREAL ATVPIGRLRK AGLLDMVLKL
3160 3170 3180 3190
AESDDTEDSA TATDDAADAL DLDDMDAEAL LRLAAENSAN
Length:3,190
Mass (Da):334,066
Last modified:December 1, 2001 - v1
Checksum:iEC005DABF792D89B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF357202 Genomic DNA. Translation: AAK73513.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF357202 Genomic DNA. Translation: AAK73513.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: October 29, 2014
This is version 82 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