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Q03133 (ERYA3_SACER) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:eryA
OrganismSaccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifier1836 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora

Protein attributes

Sequence length3172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 phosphopantetheines covalently.

NADP.

Pathway

Antibiotic biosynthesis; erythromycin biosynthesis.

Miscellaneous

In each ORF of eryA two modules are present each encoding 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.

Sequence similarities

Contains 2 acyl carrier domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 31723171Erythronolide synthase, modules 5 and 6
PRO_0000180295

Regions

Domain1394 – 146471Acyl carrier 1
Domain2821 – 289171Acyl carrier 2
Nucleotide binding1118 – 116447NADP
Nucleotide binding2557 – 260549NADP
Region2 – 14841483Module 5
Region37 – 484448Beta-ketoacyl synthase 1
Region554 – 878325Acyltransferase (AT) 1
Region1116 – 1298183Beta-ketoacyl reductase 1
Region1485 – 31721688Module 6
Region1488 – 1954467Beta-ketoacyl synthase 2
Region2021 – 2335315Acyltransferase (AT) 2
Region2555 – 2735181Beta-ketoacyl reductase 2
Region2926 – 3172247Thioesterase

Sites

Active site1991Acyl-thioester intermediate By similarity
Active site6431Acyl-ester intermediate By similarity
Active site16611Acyl-thioester intermediate By similarity
Active site21121Acyl-ester intermediate By similarity

Amino acid modifications

Modified residue14271O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residue28541O-(pantetheine 4'-phosphoryl)serine By similarity

Experimental info

Sequence conflict2891A → R in AAA26495. Ref.2
Sequence conflict493 – 51725PEPRN…MEHRA → ASRGTRCATPVSRWPPAAAP WEQ in CAA39583. Ref.1
Sequence conflict4931P → R in AAA26495. Ref.2
Sequence conflict5101A → R in AAA26495. Ref.2
Sequence conflict5131M → W in AAA26495. Ref.2
Sequence conflict5251E → D in AAA26495. Ref.2
Sequence conflict5361R → G in AAA26495. Ref.2
Sequence conflict547 – 5515GPNSP → ARTR in AAA26495. Ref.2
Sequence conflict6731R → A in AAA26495. Ref.2
Sequence conflict7161Missing in AAA26495. Ref.2
Sequence conflict734 – 7363AHK → GIT in AAA26495. Ref.2
Sequence conflict8961R → RELPVYPFQRQR in CAA39583. Ref.1
Sequence conflict8961R → RQR in AAA26495. Ref.2
Sequence conflict988 – 9947GVAAVPH → VSLLSRD in AAA26495. Ref.2
Sequence conflict1108 – 11169RTHPLEPLA → ARTRWSPR in AAA26495. Ref.2
Sequence conflict1123 – 11253Missing in CAA39583. Ref.1
Sequence conflict11321L → V in AAA26495. Ref.2
Sequence conflict11921A → R in AAA26495. Ref.2
Sequence conflict11941Missing in AAA26495. Ref.2
Sequence conflict1277 – 12782AA → RR in AAA26495. Ref.2
Sequence conflict1385 – 13906LCDGRE → STAER in AAA26495. Ref.2
Sequence conflict14851Missing in AAA26495. Ref.2
Sequence conflict15181G → R in AAA26495. Ref.2
Sequence conflict16011V → L in AAA26495. Ref.2
Sequence conflict1724 – 17252LP → FA in AAA26495. Ref.2
Sequence conflict17321Q → L in AAA26495. Ref.2
Sequence conflict1739 – 17435GPAEG → ARRA in AAA26495. Ref.2
Sequence conflict17621T → S in AAA26495. Ref.2
Sequence conflict22521D → DGAD in AAA26495. Ref.2
Sequence conflict2275 – 22773QSP → AVA in AAA26495. Ref.2
Sequence conflict24081G → GR in AAA26495. Ref.2
Sequence conflict2420 – 24212LA → S in AAA26495. Ref.2
Sequence conflict2443 – 24442NA → TH in AAA26495. Ref.2
Sequence conflict25961A → G in AAA26495. Ref.2
Sequence conflict26091P → A in AAA26495. Ref.2
Sequence conflict2715 – 27228RRAEGRAA → AVRKAVRR in CAA39583. Ref.1
Sequence conflict27541D → E in AAA26495. Ref.2

Secondary structure

1 ................................................. 3172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03133 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: DBBD5094E77DDD5F

FASTA3,172331,479
        10         20         30         40         50         60 
MSGDNGMTEE KLRRYLKRTV TELDSVTARL REVEHRAGEP IAIVGMACRF PGDVDSPESF 

        70         80         90        100        110        120 
WEFVSGGGDA IAEAPADRGW EPDPDARLGG MLAAAGDFDA GFFGISPREA LAMDPQQRIM 

       130        140        150        160        170        180 
LEISWEALER AGHDPVSLRG SATGVFTGVG TVDYGPRPDE APDEVLGYVG TGTASSVASG 

       190        200        210        220        230        240 
RVAYCLGLEG PAMTVDTACS SGLTALHLAM ESLRRDECGL ALAGGVTVMS SPGAFTEFRS 

       250        260        270        280        290        300 
QGGLAADGRC KPFSKAADGF GLAEGAGVLV LQRLSAARRE GRPVLAVLAG SAVNQDGASN 

       310        320        330        340        350        360 
GLTAPSGPAQ QRVIRRALEN AGVRAGDVDY VEAHGTGTRL GDPIEVHALL STYGAERDPD 

       370        380        390        400        410        420 
DPLWIGSVKS NIGHTQAAAG VAGVMKAVLA LRHGEMPRTL HFDEPSPQIE WDLGAVSVVS 

       430        440        450        460        470        480 
QARSWPAGER PRRAGVSSFG ISGTNAHVIV EEAPEADEPE PAPDSGPVPL VLSGRDEQAM 

       490        500        510        520        530        540 
RAQAGRLADH LAPEPRNSLR DTGFTLATRA SAMEHRAVVV GDRDEALAGL RAVADRRIAD 

       550        560        570        580        590        600 
RTATGQGPNS PRRVAMVFPG QGAQWQGMAR DLLRESQVFA DSIRDCERAL APHVDWSLTD 

       610        620        630        640        650        660 
LLSGARPLDR VDVVQPALFA VMVSLAALWR SHGVEPAAVV GHSQGEIAAA HVAGALTLED 

       670        680        690        700        710        720 
AAKLVAVRSR VLRRLGGQGG MASFGLGTEQ AAERIGRFAG ALSIASVNGP RSVVVVAGES 

       730        740        750        760        770        780 
GPLDELIAEC EAEAHKARRI PVDYASHSPQ VESLREELLT ELAGISPVSA DVALYSTTTG 

       790        800        810        820        830        840 
QPIDTATMDT AYWYANLREQ VRFQDATRQL AEAGFDAFVE VSPHPVLTVG IEATLDSALP 

       850        860        870        880        890        900 
ADAGACVVGT LRRDRGGLAD FHTALGEAYA QGVEVDWSPA FADARPVELP VYPFQRYWLP 

       910        920        930        940        950        960 
IPTGGRARDE DDDWRYQVVW REAEWESASL AGRVLLVTGP GVPSELSDAI RSGLEQSGAT 

       970        980        990       1000       1010       1020 
VLTCDVESRS TIGTALEAAD TDALSTVGVA AVPHGEAVDP SLDALALVQA LGAAGVEAPL 

      1030       1040       1050       1060       1070       1080 
WVLTRNAVQV ADGELVDPAQ AMVGGLGRVV GIEQPGRWGG LVDLVDADAA SIRSLAAVLA 

      1090       1100       1110       1120       1130       1140 
DPRGEEQVAI RADGIKVARL VPAPARARTH PLEPLAGTVL VTGGTGGIGA HLARWLARSG 

      1150       1160       1170       1180       1190       1200 
AEHLVLLGRR GADAPGASEL REELTALGTG VTIAACDVAD RARLEAVLAA EAAAEGRTVS 

      1210       1220       1230       1240       1250       1260 
AVMHAAGVST STPLDDLTEA EFTEIADVKV RGTVNLDELC PDLDAFVLFS SNAGVWGSPG 

      1270       1280       1290       1300       1310       1320 
LASYAAANAF LDGFARAARS EGAPVTSIAW GLWAGQNMAG DEGGEYLRSQ GLRAMDPDRA 

      1330       1340       1350       1360       1370       1380 
VEELHITLDH GQTSVSVVDM DRRRFVELFT AARHRPLFDE IAGARAEARQ SEEGPALAQR 

      1390       1400       1410       1420       1430       1440 
LAALLCDGRE REHLAHLIRA EVAAVLGHGD DAAIDRDRAF RDLGFDSMTA VDLRNRLAAV 

      1450       1460       1470       1480       1490       1500 
TGVREAATVV FDHPTITRLA DHYLERLVGA AEAEQAPALV REVPPKDADD PIAIVGMACR 

      1510       1520       1530       1540       1550       1560 
FPGGVHNPGE LWEFIVGGGD AVTEMPTDRG WDLDALFDPD PQRHGTSYSR HGAFLDGAAD 

      1570       1580       1590       1600       1610       1620 
FDAAFFGISP REALAMDPQQ RQVLETTWEL FENAGIDPHS VRGSDTGVFL GAAYQGYGQD 

      1630       1640       1650       1660       1670       1680 
AVVPEDSEGY LLTGNSSAVV SGRVAYVLGL EGPAVTVDTA CSSSLVALHS ACGSLRDGDC 

      1690       1700       1710       1720       1730       1740 
GLAVAGGVSV MAGPEVFTEF SRQGGLAVDG RCKAFSAEAD GFGLPEGVAV VQLQRLSDGP 

      1750       1760       1770       1780       1790       1800 
AEGGRQVLGV VAGSAINQDG ATNGLAAPSG VAQQRVIRKA WARAGITGAD VAVVEAHGTG 

      1810       1820       1830       1840       1850       1860 
TRLGDPVEAS ALLATYGKSR GSSGPVLLGS VKSNIGHAQA AAGVAGVIKV VLGLNRGLVP 

      1870       1880       1890       1900       1910       1920 
PMLCRGERSP LIEWSSGGVE LAEAVSPWPP AADGVRRAGV SAFGVSGTNA HVIIAEPPEP 

      1930       1940       1950       1960       1970       1980 
EPLPEPGPVG VLAAANSVPV LLSARTETAL AAQARLLESA VDDSVPLTAL ASALATGRAH 

      1990       2000       2010       2020       2030       2040 
LPRRAALLAG DHEQLRGQLR AVAEGVAAPG ATTGTASAGG VVFVFPGQGA QWEGMARGLL 

      2050       2060       2070       2080       2090       2100 
SVPVFAESIA ECDAVLSEVA GFSASEVLEQ RPDAPSLERV DVVQPVLFSV MVSLARLWGA 

      2110       2120       2130       2140       2150       2160 
CGVSPSAVIG HSQGEIAAAV VAGVLSLEDG VRVVALRAKA LRALAGKGGM VSLAAPGERA 

      2170       2180       2190       2200       2210       2220 
RALIAPWEDR ISVAAVNSPS SVVVSGDPEA LAELVARCED EGVRAKTLPV DYASHSRHVE 

      2230       2240       2250       2260       2270       2280 
EIRETILADL DGISARRAAI PLYSTLHGER RDMGPRYWYD NLRSQVRFDE AVSAQSPDGH 

      2290       2300       2310       2320       2330       2340 
ATFVEMSPHP VLTAAVQEIA ADAVAIGSLH RDTAEEHLIA ELARAHVHGV AVDWRNVFPA 

      2350       2360       2370       2380       2390       2400 
APPVALPNYP FEPQRYWLAP EVSDQLADSR YRVDWRPLAT TPVDLEGGFL VHGSAPESLT 

      2410       2420       2430       2440       2450       2460 
SAVEKAGGVV PVASADREAL AAALREVPGE VAGVLSVHTG AANALALHQS LGEAGVRAPL 

      2470       2480       2490       2500       2510       2520 
WLVTSRAVAL GESEPVDPEQ AMVWGLGRVM GLETPERWGG LVDLPAEPAP GDGEAFVACL 

      2530       2540       2550       2560       2570       2580 
GADGHEDQVA IRDHARYGRR LVRAPLGTRE SSWEPAGTAL VTGGTGALGG HVARHLARCG 

      2590       2600       2610       2620       2630       2640 
VEDLVLVSRR GVDAPAAAEL EAELVALGPK TTITACDVAD REQLSKLLEE LRGQGRPVRT 

      2650       2660       2670       2680       2690       2700 
VVHTAGVPES RPLHEIGELE SVCAAKVTGA RLLDELCPDA ETFVLFSSGA GVWGSANLGA 

      2710       2720       2730       2740       2750       2760 
YSAANAYLDA LAHRRRAEGR AATSVAWGAW AGEGMATGDL EGLTRRGLRP MAPDRAIRAL 

      2770       2780       2790       2800       2810       2820 
HQALDNGDTC VSIADVDWEA FAVGFTAARP RPLLDELVTP AVGAVPAVQA APAREMTSQE 

      2830       2840       2850       2860       2870       2880 
LLEFTHSHVA AILGHSSPDA VGQDQPFTEL GFDSLTAVGL RNQLQQATGL ALPATLVFEH 

      2890       2900       2910       2920       2930       2940 
PTVRRLADHI GQQLDSGTPA REASSALRDG YRQAGVSGRV RSYLDLLAGL SDFREHFDGS 

      2950       2960       2970       2980       2990       3000 
DGFSLDLVDM ADGPGEVTVI CCAGTAAISG PHEFTRLAGA LRGIAPVRAV PQPGYEEGEP 

      3010       3020       3030       3040       3050       3060 
LPSSMAAVAA VQADAVIRTQ GDKPFVVAGH SAGALMAYAL ATELLDRGHP PRGVVLIDVY 

      3070       3080       3090       3100       3110       3120 
PPGHQDAMNA WLEELTATLF DRETVRMDDT RLTALGAYDR LTGQWRPRET GLPTLLVSAG 

      3130       3140       3150       3160       3170 
EPMGPWPDDS WKPTWPFEHD TVAVPGDHFT MVQEHADAIA RHIDAWLGGG NS

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56107 Genomic DNA. Translation: CAA39583.1.
M63677 Genomic DNA. Translation: AAA26495.1.
X62569 Genomic DNA. Translation: CAA44449.1.
PIRS13595.
S22012.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ03133.
SMRQ03133. Positions 1-901, 2904-3170.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17079.
UniPathwayUPA00240.

Family and domain databases

Gene3D1.10.1200.10. 2 hits.
3.40.366.10. 4 hits.
3.40.47.10. 4 hits.
3.40.50.720. 2 hits.
InterProIPR001227. 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]
PfamPF00698. 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]
SMARTSM00827. 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]
SUPFAMSSF47336. ACP_like. 2 hits.
SSF52151. Acyl_Trfase/lysoPlipase. 2 hits.
SSF55048. Malonyl_transacylase_ACP-bd. 2 hits.
SSF101173. Polyketide_synth_docking. 1 hit.
SSF53901. Thiolase-like. 2 hits.
PROSITEPS50075. ACP_DOMAIN. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03133.

Entry information

Entry nameERYA3_SACER
AccessionPrimary (citable) accession number: Q03133
Secondary accession number(s): Q54097, Q99270
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 109 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents