UniProtKB - Q4WF53 (SIDD_ASPFU)
Nonribosomal peptide synthase sidD
NRPS4
Functioni
Nonribosomal peptide synthase; part of the siderophore biosynthetic pathway (PubMed:15953695, PubMed:17845073, PubMed:17464044).
Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N2-acetyl-N5-anhydromevalonyl-N5-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265).
Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073).
For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N5-hydroxyornithine (PubMed:17845073).
The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303).
The acetylation of N5-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789).
FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073).
Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:15953695, PubMed:17845073, PubMed:17464044).
Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073).
Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
7 Publications: Siderophore biosynthesis Pathwayi
This protein is involved in Siderophore biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in Siderophore biosynthesis.
GO - Molecular functioni
- ligase activity Source: UniProtKB-KW
- phosphopantetheine binding Source: GO_Central
GO - Biological processi
- amino acid activation for nonribosomal peptide biosynthetic process Source: GO_Central
- cellular response to iron ion starvation Source: AspGD
- ergosterol biosynthetic process Source: AspGD
- N',N'',N'''-triacetylfusarinine C biosynthetic process Source: AspGD
- nonribosomal peptide biosynthetic process Source: AspGD
- secondary metabolic process Source: AspGD
- secondary metabolite biosynthetic process Source: AspGD
Keywordsi
Molecular function | Ligase |
Biological process | Virulence |
Names & Taxonomyi
Protein namesi | Recommended name: Nonribosomal peptide synthase sidD1 Publication (EC:6.3.2.-1 Publication)Short name: NPRS sidD1 Publication Alternative name(s): Siderophore synthetase D1 Publication |
Gene namesi | Name:NRPS41 Publication Synonyms:sidD1 Publication ORF Names:AFUA_3G03420 |
Organismi | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic identifieri | 330879 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati › |
Proteomesi |
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Organism-specific databases
VEuPathDBi | FungiDB:Afu3g03420 |
Pathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000416545 | 1 – 2083 | Nonribosomal peptide synthase sidDAdd BLAST | 2083 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 801 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 | |
Modified residuei | 1594 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Phosphopantetheine, PhosphoproteinProteomic databases
PRIDEi | Q4WF53 |
Expressioni
Inductioni
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 764 – 840 | Carrier 1PROSITE-ProRule annotationAdd BLAST | 77 | |
Domaini | 1557 – 1633 | Carrier 2PROSITE-ProRule annotationAdd BLAST | 77 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 251 – 650 | Adenylation 1Add BLAST | 400 | |
Regioni | 876 – 1146 | Condensation 1Add BLAST | 271 | |
Regioni | 1336 – 1421 | Adenylation 2Add BLAST | 86 | |
Regioni | 1674 – 1946 | Condensation 2Add BLAST | 273 |
Domaini
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG1178, Eukaryota |
HOGENOMi | CLU_000022_60_2_1 |
InParanoidi | Q4WF53 |
OMAi | FNPYPLM |
OrthoDBi | 4243at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.30.300.30, 2 hits 3.30.559.10, 2 hits 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF00668, Condensation, 2 hits PF00550, PP-binding, 2 hits |
SMARTi | View protein in SMART SM00823, PKS_PP, 2 hits |
SUPFAMi | SSF47336, SSF47336, 2 hits |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit PS50075, CARRIER, 2 hits |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MGSIQQDDVH NQIDHCNQSD DLPAARLNCN DVELFEVAGL ACDETSSPTG
60 70 80 90 100
MRDEMVLLSW LIALLRTREG GQIRYEWAYR YPEEEPVPRC LAMNEVVAGL
110 120 130 140 150
QSSVKETAAA VSRHISADVS SPPAPASLLL STSSLSQTSD EAKDEGLLHL
160 170 180 190 200
EIAFENGLCK IRPTWHSENM LPFTVTRYAR TLIDTVRLCI SNCDAAIQDC
210 220 230 240 250
LRPTAYDLDE IWRWNHNLPP TYNFCMHEII SDQAQKFPDK EAIASWDGSL
260 270 280 290 300
TYRQIDQYSS FVARSLIGMG VGLHDVLPVC FEKSRWTIVA VLAVMKAGAT
310 320 330 340 350
FVLMDPTLPL ARLQNMAQQV GAKMMVSSRG QYNLATEIIP NANVLVVEEN
360 370 380 390 400
TFSSLSAEQN GEPLPTVPSS ALMYMIFTSG STGTPKGVKI SHETYTSSAI
410 420 430 440 450
PRANAVGYTE DSRVLDFASY AFDVSIDSML LTLGNGGCLC IPSDEDRLND
460 470 480 490 500
INGVIRRMKV NYAGLTPSVA RILDADVISS LSGLGLGGEA VSARDVNLWG
510 520 530 540 550
QDTRIIIGYG PCECTIGCTV NSSAATGRDY ISIGPGNGAV IWIVDPNDHE
560 570 580 590 600
SLVPLGAVGE LLVEGPIVGQ GYLNDPEKTA AAFIEDPSWL VAGHEGYPGR
610 620 630 640 650
RGRLYKTGDL GRYDPDGSGG IVFVGRKDTQ VKLRGQRVEL GEIESQLRAR
660 670 680 690 700
LPSETTVIAE VIVPQGSGGQ PTLVAFVAAQ TTKGHDHTGL EAAELPDELR
710 720 730 740 750
RALSEADAEL AKVLPRYMVP TAYIPVNHIP TLISGKTDRK RLRQFGATVD
760 770 780 790 800
LRQLDQDATN TAARELSDLE RRLRQAWSQT LKLQACSIRL QDNFFALGGD
810 820 830 840 850
SLTAMKLVSV CRSQGLDLSV TSMFSNPTLS AMASVVRICD VDVQRTVPAF
860 870 880 890 900
SMITSDMNSA CVEAAEPCGV GPADIEDIYP CTPTQESLFT FSLKSVKPYV
910 920 930 940 950
AQRVLCIPSH IDLNAWRKAW EDVVAALPIL RTRVAQLQEP GLQQVVLKNS
960 970 980 990 1000
ISWTQASDLA EYLENDRTQK MNLGESLARY AIVEDSADGK RYMVWTIHHV
1010 1020 1030 1040 1050
LYDGWSEPII LKQVSDALQG QPVEVKAQMR DFVRFVRDSD DAAVQEFWRR
1060 1070 1080 1090 1100
ELKGAVGPQF PRLPSRDFMP TPDALVERQV SLDTSSGSPF TMATLIRGAW
1110 1120 1130 1140 1150
ALVASQYTGS DDIVFGETLT GRDIPLPGVE SIVGPLIATV PIRVRILRGS
1160 1170 1180 1190 1200
TVESYLQAVQ QSVLARTPYQ HLGMQNIRKV SQDAQHACET GTGLVIQPEP
1210 1220 1230 1240 1250
EYVGSELGVE RGDVVLEALH FNPYPLMLAC GIRKGGFRVC ASFDSSLIET
1260 1270 1280 1290 1300
RQMERMLAQL ETACWQLSQG LSRKVDEISC LPEAELNQIW QWNRSPPLSL
1310 1320 1330 1340 1350
DETTSRLRAN ASTKPGSSYP PAVVPWVCSP RNSSLLSPIG CVGELWLEGA
1360 1370 1380 1390 1400
LLSGDTVDSP AWLVAGSSTC AGRTGKVQAT GDMVQLREDG SLVFVGRKEN
1410 1420 1430 1440 1450
VVPVQGHAVD ITEIERHLAE HLPPTIRAAA TVVRSSSDQE LVMFIEQPAA
1460 1470 1480 1490 1500
EEACIELLSE KREIVCDAPD KAFQTTICAT IPGSLAAVLK KLDKYMRDSL
1510 1520 1530 1540 1550
PSYMAPSAYI VVEKLPNTMD DIDHNLLNQI ASQVTPQILN ELRDGLSNAW
1560 1570 1580 1590 1600
TKATAPNHLS ASESILRSAW AKVLRVDPEQ IDVDDNFFRR GGDSVLAMKL
1610 1620 1630 1640 1650
VSSLRAQGYS LSVADIFRHM RLSDAARVMK VDERSTEKIN SYQPFSMLRL
1660 1670 1680 1690 1700
PDVQQFLANI VRPQLGDQHW PIRDVLPVTD SQDMDIRATI QPPRTSIQYT
1710 1720 1730 1740 1750
MLYFDNSVDR ERLFRSCSDL VKTHEILRTV FISHESSFLQ VVLNELEIPV
1760 1770 1780 1790 1800
RAHKTDKQLD QYVASLFRED IESNFQLGCP FLRLFYVEGN NGESCLVIGL
1810 1820 1830 1840 1850
SHAQYDGVSL PRLLQDLDAL YTGTQLATFS PFSLYMAQTS EEAIQNKAAA
1860 1870 1880 1890 1900
YWRNLLSSSS LSTLDGPSSD PTDKAIFHTR PVNIHPLKEI TTANLLTAAW
1910 1920 1930 1940 1950
AMVLARRLQT PDVTFGSVTS GRTLDIPNAE NFMGPCYQLT PVRVPFHPDW
1960 1970 1980 1990 2000
TASDLLNFVQ TQSAESAAHD FLGFEKIAKL AGWASGRQGF DSIVHHQDWE
2010 2020 2030 2040 2050
DFDMMPFGGG SCRVDIANPH GDAAYPVKAV SFVKEGEIHV GVVCSERDVM
2060 2070 2080
FVDEVLGELA AAVVELAGQS TEVLLDSKLF SGQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000010 Genomic DNA Translation: EAL86624.1 |
RefSeqi | XP_748662.1, XM_743569.1 |
Genome annotation databases
EnsemblFungii | EAL86624; EAL86624; AFUA_3G03420 |
GeneIDi | 3506154 |
KEGGi | afm:AFUA_3G03420 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000010 Genomic DNA Translation: EAL86624.1 |
RefSeqi | XP_748662.1, XM_743569.1 |
3D structure databases
SMRi | Q4WF53 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 746128.CADAFUBP00004398 |
Proteomic databases
PRIDEi | Q4WF53 |
Genome annotation databases
EnsemblFungii | EAL86624; EAL86624; AFUA_3G03420 |
GeneIDi | 3506154 |
KEGGi | afm:AFUA_3G03420 |
Organism-specific databases
VEuPathDBi | FungiDB:Afu3g03420 |
Phylogenomic databases
eggNOGi | KOG1178, Eukaryota |
HOGENOMi | CLU_000022_60_2_1 |
InParanoidi | Q4WF53 |
OMAi | FNPYPLM |
OrthoDBi | 4243at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 2 hits 3.30.300.30, 2 hits 3.30.559.10, 2 hits 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF00668, Condensation, 2 hits PF00550, PP-binding, 2 hits |
SMARTi | View protein in SMART SM00823, PKS_PP, 2 hits |
SUPFAMi | SSF47336, SSF47336, 2 hits |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit PS50075, CARRIER, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | SIDD_ASPFU | |
Accessioni | Q4WF53Primary (citable) accession number: Q4WF53 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 18, 2012 |
Last sequence update: | July 5, 2005 | |
Last modified: | February 23, 2022 | |
This is version 95 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families