SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q03133

- ERYA3_SACER

UniProt

Q03133 - ERYA3_SACER

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Erythronolide synthase, modules 5 and 6
Gene
eryA
Organism
Saccharopolyspora erythraea (Streptomyces erythraeus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+.

Cofactori

Binds 2 phosphopantetheines covalently.
NADP.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei199 – 1991Acyl-thioester intermediate By similarity
Active sitei643 – 6431Acyl-ester intermediate By similarity
Active sitei1661 – 16611Acyl-thioester intermediate By similarity
Active sitei2112 – 21121Acyl-ester intermediate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1118 – 116447NADP
Add
BLAST
Nucleotide bindingi2557 – 260549NADP
Add
BLAST

GO - Molecular functioni

  1. cofactor binding Source: InterPro
  2. erythronolide synthase activity Source: UniProtKB-EC
  3. hydrolase activity, acting on ester bonds Source: InterPro
  4. oxidoreductase activity Source: InterPro
  5. phosphopantetheine binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17079.
UniPathwayiUPA00240.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythronolide synthase, modules 5 and 6 (EC:2.3.1.94)
Alternative name(s):
6-deoxyerythronolide B synthase III
DEBS 3
ORF 3
Gene namesi
Name:eryA
OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifieri1836 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 31723171Erythronolide synthase, modules 5 and 6
PRO_0000180295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1427 – 14271O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residuei2854 – 28541O-(pantetheine 4'-phosphoryl)serine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3829
Beta strandi41 – 5010
Turni51 – 533
Helixi57 – 659
Helixi76 – 783
Beta strandi88 – 903
Turni93 – 964
Helixi101 – 1033
Helixi107 – 1126
Helixi115 – 13016
Helixi135 – 1384
Beta strandi143 – 1497
Helixi163 – 1686
Helixi169 – 1735
Helixi175 – 18612
Beta strandi192 – 1965
Helixi198 – 2003
Helixi201 – 21414
Beta strandi219 – 2279
Helixi233 – 2386
Beta strandi265 – 2739
Helixi274 – 2796
Beta strandi286 – 29510
Beta strandi300 – 3034
Helixi307 – 32115
Helixi325 – 3273
Beta strandi330 – 3323
Helixi341 – 35010
Turni351 – 3555
Beta strandi364 – 3663
Helixi369 – 3724
Helixi376 – 3783
Helixi381 – 39313
Beta strandi433 – 4397
Beta strandi443 – 45210
Beta strandi468 – 4769
Helixi477 – 49317
Helixi499 – 50810
Beta strandi514 – 5229
Helixi523 – 53412
Beta strandi542 – 5465
Beta strandi554 – 5585
Helixi570 – 5756
Helixi577 – 59014
Helixi591 – 5933
Helixi598 – 6036
Helixi611 – 63121
Beta strandi637 – 6415
Helixi645 – 6528
Helixi658 – 67114
Helixi672 – 6754
Beta strandi680 – 6867
Helixi688 – 6958
Helixi696 – 6983
Beta strandi701 – 7099
Beta strandi714 – 7185
Helixi722 – 73312
Beta strandi737 – 7415
Helixi749 – 7546
Helixi755 – 7617
Beta strandi771 – 7744
Turni777 – 7793
Helixi785 – 7873
Helixi790 – 7989
Helixi803 – 81210
Beta strandi817 – 8204
Beta strandi822 – 8243
Helixi828 – 83811
Beta strandi846 – 8483
Helixi858 – 86912
Turni870 – 8723
Helixi878 – 8803
Helixi2909 – 29179
Helixi2921 – 293111
Beta strandi2938 – 29414
Beta strandi2948 – 29514
Beta strandi2956 – 29616
Beta strandi2966 – 29683
Turni2971 – 29744
Helixi2975 – 29806
Beta strandi2982 – 29843
Beta strandi2987 – 29904
Beta strandi3001 – 30044
Helixi3005 – 301915
Beta strandi3021 – 30233
Beta strandi3025 – 30284
Helixi3032 – 304312
Turni3044 – 30485
Beta strandi3052 – 30554
Turni3062 – 30643
Helixi3066 – 307611
Helixi3077 – 30793
Helixi3089 – 310113
Turni3102 – 31043
Beta strandi3114 – 31218
Beta strandi3140 – 31467
Turni3148 – 31503
Beta strandi3151 – 31544
Helixi3157 – 316711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KEZX-ray2.80A/B/C2893-3172[»]
1MO2X-ray3.00A/B2893-3172[»]
1PZRNMR-A/B1-39[»]
2HG4X-ray2.73A/B/C/D/E/F1-917[»]
ProteinModelPortaliQ03133.
SMRiQ03133. Positions 1-901, 2904-3170.

Miscellaneous databases

EvolutionaryTraceiQ03133.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1394 – 146471Acyl carrier 1
Add
BLAST
Domaini2821 – 289171Acyl carrier 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 14841483Module 5
Add
BLAST
Regioni37 – 484448Beta-ketoacyl synthase 1
Add
BLAST
Regioni554 – 878325Acyltransferase (AT) 1
Add
BLAST
Regioni1116 – 1298183Beta-ketoacyl reductase 1
Add
BLAST
Regioni1485 – 31721688Module 6
Add
BLAST
Regioni1488 – 1954467Beta-ketoacyl synthase 2
Add
BLAST
Regioni2021 – 2335315Acyltransferase (AT) 2
Add
BLAST
Regioni2555 – 2735181Beta-ketoacyl reductase 2
Add
BLAST
Regioni2926 – 3172247Thioesterase
Add
BLAST

Sequence similaritiesi

Contains 2 acyl carrier domains.

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.1820. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR029058. AB_hydrolase.
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.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 2 hits.
PF00106. adh_short. 2 hits.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF00550. PP-binding. 2 hits.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 2 hits.
SM00822. PKS_KR. 2 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 2 hits.
SSF52151. SSF52151. 4 hits.
SSF53474. SSF53474. 2 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03133-1 [UniParc]FASTAAdd to Basket

« Hide

MSGDNGMTEE KLRRYLKRTV TELDSVTARL REVEHRAGEP IAIVGMACRF     50
PGDVDSPESF WEFVSGGGDA IAEAPADRGW EPDPDARLGG MLAAAGDFDA 100
GFFGISPREA LAMDPQQRIM LEISWEALER AGHDPVSLRG SATGVFTGVG 150
TVDYGPRPDE APDEVLGYVG TGTASSVASG RVAYCLGLEG PAMTVDTACS 200
SGLTALHLAM ESLRRDECGL ALAGGVTVMS SPGAFTEFRS QGGLAADGRC 250
KPFSKAADGF GLAEGAGVLV LQRLSAARRE GRPVLAVLAG SAVNQDGASN 300
GLTAPSGPAQ QRVIRRALEN AGVRAGDVDY VEAHGTGTRL GDPIEVHALL 350
STYGAERDPD DPLWIGSVKS NIGHTQAAAG VAGVMKAVLA LRHGEMPRTL 400
HFDEPSPQIE WDLGAVSVVS QARSWPAGER PRRAGVSSFG ISGTNAHVIV 450
EEAPEADEPE PAPDSGPVPL VLSGRDEQAM RAQAGRLADH LAPEPRNSLR 500
DTGFTLATRA SAMEHRAVVV GDRDEALAGL RAVADRRIAD RTATGQGPNS 550
PRRVAMVFPG QGAQWQGMAR DLLRESQVFA DSIRDCERAL APHVDWSLTD 600
LLSGARPLDR VDVVQPALFA VMVSLAALWR SHGVEPAAVV GHSQGEIAAA 650
HVAGALTLED AAKLVAVRSR VLRRLGGQGG MASFGLGTEQ AAERIGRFAG 700
ALSIASVNGP RSVVVVAGES GPLDELIAEC EAEAHKARRI PVDYASHSPQ 750
VESLREELLT ELAGISPVSA DVALYSTTTG QPIDTATMDT AYWYANLREQ 800
VRFQDATRQL AEAGFDAFVE VSPHPVLTVG IEATLDSALP ADAGACVVGT 850
LRRDRGGLAD FHTALGEAYA QGVEVDWSPA FADARPVELP VYPFQRYWLP 900
IPTGGRARDE DDDWRYQVVW REAEWESASL AGRVLLVTGP GVPSELSDAI 950
RSGLEQSGAT VLTCDVESRS TIGTALEAAD TDALSTVGVA AVPHGEAVDP 1000
SLDALALVQA LGAAGVEAPL WVLTRNAVQV ADGELVDPAQ AMVGGLGRVV 1050
GIEQPGRWGG LVDLVDADAA SIRSLAAVLA DPRGEEQVAI RADGIKVARL 1100
VPAPARARTH PLEPLAGTVL VTGGTGGIGA HLARWLARSG AEHLVLLGRR 1150
GADAPGASEL REELTALGTG VTIAACDVAD RARLEAVLAA EAAAEGRTVS 1200
AVMHAAGVST STPLDDLTEA EFTEIADVKV RGTVNLDELC PDLDAFVLFS 1250
SNAGVWGSPG LASYAAANAF LDGFARAARS EGAPVTSIAW GLWAGQNMAG 1300
DEGGEYLRSQ GLRAMDPDRA VEELHITLDH GQTSVSVVDM DRRRFVELFT 1350
AARHRPLFDE IAGARAEARQ SEEGPALAQR LAALLCDGRE REHLAHLIRA 1400
EVAAVLGHGD DAAIDRDRAF RDLGFDSMTA VDLRNRLAAV TGVREAATVV 1450
FDHPTITRLA DHYLERLVGA AEAEQAPALV REVPPKDADD PIAIVGMACR 1500
FPGGVHNPGE LWEFIVGGGD AVTEMPTDRG WDLDALFDPD PQRHGTSYSR 1550
HGAFLDGAAD FDAAFFGISP REALAMDPQQ RQVLETTWEL FENAGIDPHS 1600
VRGSDTGVFL GAAYQGYGQD AVVPEDSEGY LLTGNSSAVV SGRVAYVLGL 1650
EGPAVTVDTA CSSSLVALHS ACGSLRDGDC GLAVAGGVSV MAGPEVFTEF 1700
SRQGGLAVDG RCKAFSAEAD GFGLPEGVAV VQLQRLSDGP AEGGRQVLGV 1750
VAGSAINQDG ATNGLAAPSG VAQQRVIRKA WARAGITGAD VAVVEAHGTG 1800
TRLGDPVEAS ALLATYGKSR GSSGPVLLGS VKSNIGHAQA AAGVAGVIKV 1850
VLGLNRGLVP PMLCRGERSP LIEWSSGGVE LAEAVSPWPP AADGVRRAGV 1900
SAFGVSGTNA HVIIAEPPEP EPLPEPGPVG VLAAANSVPV LLSARTETAL 1950
AAQARLLESA VDDSVPLTAL ASALATGRAH LPRRAALLAG DHEQLRGQLR 2000
AVAEGVAAPG ATTGTASAGG VVFVFPGQGA QWEGMARGLL SVPVFAESIA 2050
ECDAVLSEVA GFSASEVLEQ RPDAPSLERV DVVQPVLFSV MVSLARLWGA 2100
CGVSPSAVIG HSQGEIAAAV VAGVLSLEDG VRVVALRAKA LRALAGKGGM 2150
VSLAAPGERA RALIAPWEDR ISVAAVNSPS SVVVSGDPEA LAELVARCED 2200
EGVRAKTLPV DYASHSRHVE EIRETILADL DGISARRAAI PLYSTLHGER 2250
RDMGPRYWYD NLRSQVRFDE AVSAQSPDGH ATFVEMSPHP VLTAAVQEIA 2300
ADAVAIGSLH RDTAEEHLIA ELARAHVHGV AVDWRNVFPA APPVALPNYP 2350
FEPQRYWLAP EVSDQLADSR YRVDWRPLAT TPVDLEGGFL VHGSAPESLT 2400
SAVEKAGGVV PVASADREAL AAALREVPGE VAGVLSVHTG AANALALHQS 2450
LGEAGVRAPL WLVTSRAVAL GESEPVDPEQ AMVWGLGRVM GLETPERWGG 2500
LVDLPAEPAP GDGEAFVACL GADGHEDQVA IRDHARYGRR LVRAPLGTRE 2550
SSWEPAGTAL VTGGTGALGG HVARHLARCG VEDLVLVSRR GVDAPAAAEL 2600
EAELVALGPK TTITACDVAD REQLSKLLEE LRGQGRPVRT VVHTAGVPES 2650
RPLHEIGELE SVCAAKVTGA RLLDELCPDA ETFVLFSSGA GVWGSANLGA 2700
YSAANAYLDA LAHRRRAEGR AATSVAWGAW AGEGMATGDL EGLTRRGLRP 2750
MAPDRAIRAL HQALDNGDTC VSIADVDWEA FAVGFTAARP RPLLDELVTP 2800
AVGAVPAVQA APAREMTSQE LLEFTHSHVA AILGHSSPDA VGQDQPFTEL 2850
GFDSLTAVGL RNQLQQATGL ALPATLVFEH PTVRRLADHI GQQLDSGTPA 2900
REASSALRDG YRQAGVSGRV RSYLDLLAGL SDFREHFDGS DGFSLDLVDM 2950
ADGPGEVTVI CCAGTAAISG PHEFTRLAGA LRGIAPVRAV PQPGYEEGEP 3000
LPSSMAAVAA VQADAVIRTQ GDKPFVVAGH SAGALMAYAL ATELLDRGHP 3050
PRGVVLIDVY PPGHQDAMNA WLEELTATLF DRETVRMDDT RLTALGAYDR 3100
LTGQWRPRET GLPTLLVSAG EPMGPWPDDS WKPTWPFEHD TVAVPGDHFT 3150
MVQEHADAIA RHIDAWLGGG NS 3172
Length:3,172
Mass (Da):331,479
Last modified:January 23, 2007 - v4
Checksum:iDBBD5094E77DDD5F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891A → R in AAA26495. 1 Publication
Sequence conflicti493 – 51725PEPRN…MEHRA → ASRGTRCATPVSRWPPAAAP WEQ in CAA39583. 1 Publication
Add
BLAST
Sequence conflicti493 – 4931P → R in AAA26495. 1 Publication
Sequence conflicti510 – 5101A → R in AAA26495. 1 Publication
Sequence conflicti513 – 5131M → W in AAA26495. 1 Publication
Sequence conflicti525 – 5251E → D in AAA26495. 1 Publication
Sequence conflicti536 – 5361R → G in AAA26495. 1 Publication
Sequence conflicti547 – 5515GPNSP → ARTR in AAA26495. 1 Publication
Sequence conflicti673 – 6731R → A in AAA26495. 1 Publication
Sequence conflicti716 – 7161Missing in AAA26495. 1 Publication
Sequence conflicti734 – 7363AHK → GIT in AAA26495. 1 Publication
Sequence conflicti896 – 8961R → RELPVYPFQRQR in CAA39583. 1 Publication
Sequence conflicti896 – 8961R → RQR in AAA26495. 1 Publication
Sequence conflicti988 – 9947GVAAVPH → VSLLSRD in AAA26495. 1 Publication
Sequence conflicti1108 – 11169RTHPLEPLA → ARTRWSPR in AAA26495. 1 Publication
Sequence conflicti1123 – 11253Missing in CAA39583. 1 Publication
Sequence conflicti1132 – 11321L → V in AAA26495. 1 Publication
Sequence conflicti1192 – 11921A → R in AAA26495. 1 Publication
Sequence conflicti1194 – 11941Missing in AAA26495. 1 Publication
Sequence conflicti1277 – 12782AA → RR in AAA26495. 1 Publication
Sequence conflicti1385 – 13906LCDGRE → STAER in AAA26495. 1 Publication
Sequence conflicti1485 – 14851Missing in AAA26495. 1 Publication
Sequence conflicti1518 – 15181G → R in AAA26495. 1 Publication
Sequence conflicti1601 – 16011V → L in AAA26495. 1 Publication
Sequence conflicti1724 – 17252LP → FA in AAA26495. 1 Publication
Sequence conflicti1732 – 17321Q → L in AAA26495. 1 Publication
Sequence conflicti1739 – 17435GPAEG → ARRA in AAA26495. 1 Publication
Sequence conflicti1762 – 17621T → S in AAA26495. 1 Publication
Sequence conflicti2252 – 22521D → DGAD in AAA26495. 1 Publication
Sequence conflicti2275 – 22773QSP → AVA in AAA26495. 1 Publication
Sequence conflicti2408 – 24081G → GR in AAA26495. 1 Publication
Sequence conflicti2420 – 24212LA → S in AAA26495. 1 Publication
Sequence conflicti2443 – 24442NA → TH in AAA26495. 1 Publication
Sequence conflicti2596 – 25961A → G in AAA26495. 1 Publication
Sequence conflicti2609 – 26091P → A in AAA26495. 1 Publication
Sequence conflicti2715 – 27228RRAEGRAA → AVRKAVRR in CAA39583. 1 Publication
Sequence conflicti2754 – 27541D → E in AAA26495. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56107 Genomic DNA. Translation: CAA39583.1.
M63677 Genomic DNA. Translation: AAA26495.1.
X62569 Genomic DNA. Translation: CAA44449.1.
PIRiS13595.
S22012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56107 Genomic DNA. Translation: CAA39583.1 .
M63677 Genomic DNA. Translation: AAA26495.1 .
X62569 Genomic DNA. Translation: CAA44449.1 .
PIRi S13595.
S22012.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KEZ X-ray 2.80 A/B/C 2893-3172 [» ]
1MO2 X-ray 3.00 A/B 2893-3172 [» ]
1PZR NMR - A/B 1-39 [» ]
2HG4 X-ray 2.73 A/B/C/D/E/F 1-917 [» ]
ProteinModelPortali Q03133.
SMRi Q03133. Positions 1-901, 2904-3170.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00240 .
BioCyci MetaCyc:MONOMER-17079.

Miscellaneous databases

EvolutionaryTracei Q03133.

Family and domain databases

Gene3Di 1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.1820. 1 hit.
3.40.50.720. 2 hits.
InterProi IPR029058. AB_hydrolase.
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.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 2 hits.
PF00106. adh_short. 2 hits.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 2 hits.
PF02801. Ketoacyl-synt_C. 2 hits.
PF00550. PP-binding. 2 hits.
PF00975. Thioesterase. 1 hit.
[Graphical view ]
SMARTi SM00827. PKS_AT. 2 hits.
SM00822. PKS_KR. 2 hits.
SM00825. PKS_KS. 2 hits.
SM00823. PKS_PP. 2 hits.
SM00824. PKS_TE. 1 hit.
[Graphical view ]
SUPFAMi SSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 2 hits.
SSF52151. SSF52151. 4 hits.
SSF53474. SSF53474. 2 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. "An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea."
    Cortes J., Haydock S.F., Roberts G.A., Bevitt D.J., Leadlay P.F.
    Nature 348:176-178(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11635 / DSM 40517 / IFO 13426 / JCM 4026 / NCIB 8594.
  2. "Modular organization of genes required for complex polyketide biosynthesis."
    Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L.
    Science 252:675-679(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "6-deoxyerythronolide-B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme."
    Bevitt D.J., Cortes J., Haydock S.F., Leadlay P.F.
    Eur. J. Biochem. 204:39-49(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11635 / DSM 40517 / IFO 13426 / JCM 4026 / NCIB 8594.
  4. "Identification of DEBS 1, DEBS 2 and DEBS 3, the multienzyme polypeptides of the erythromycin-producing polyketide synthase from Saccharopolyspora erythraea."
    Caffrey P., Bevitt D.J., Staunton J., Leadlay P.F.
    FEBS Lett. 304:225-228(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: CA340.
  5. "Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel."
    Tsai S.-C., Miercke L.J.W., Krucinski J., Gokhale R., Chen J.C.-H., Foster P.G., Cane D.E., Khosla C., Stroud R.M.
    Proc. Natl. Acad. Sci. U.S.A. 98:14808-14813(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2890-3172.
  6. "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 (3.0 ANGSTROMS) OF 2890-3172.

Entry informationi

Entry nameiERYA3_SACER
AccessioniPrimary (citable) accession number: Q03133
Secondary accession number(s): Q54097, Q99270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In each ORF of eryA two modules are present each coding for a functional synthase subunit. Thus eryA showing 3 ORFs codes for 6 synthase subunits. It is supposed that each synthase participates in one of the six FAS-like elongation steps required for formation of the polyketide. Module 1, 2, 3, 4, 5, and 6 participating in biosynthesis steps 1, 2, 3, 4, 5, and 6, respectively.
Biosynthesis of polyketides; acyltransferase (AT), beta-ketoacyl carrier protein synthase (KS), and acyl carrier protein (ACP) for chain elongation. Beta-ketoreductase (KR), dehydratase (DH), and enoyl reductase (ER) for processing of the beta carbon, and thioesterase (TE) for release and lactonization of the full-length chain.

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi