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Q9R9J1

- MYCA_BACIU

UniProt

Q9R9J1 - MYCA_BACIU

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Protein
Mycosubtilin synthase subunit A
Gene
mycA
Organism
Bacillus subtilis
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

This protein is a multifunctional enzyme, able to activate a long chain fatty acid and link it with the amino acid Asn as part of the synthesis of mycosubtilin. The activation sites consist of individual domains.1 Publication

Cofactori

Pyridoxal phosphate.1 Publication
Binds 2 phosphopantetheines covalently Reviewed prediction.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei843 – 8431For beta-ketoacyl synthase activity By similarity

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. phosphopantetheine binding Source: InterPro
  3. pyridoxal phosphate binding Source: InterPro
  4. transaminase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ligase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Mycosubtilin synthase subunit A (EC:2.3.1.-)
Including the following 2 domains:
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
ATP-dependent asparagine adenylase 1
Short name:
AsnA 1
Alternative name(s):
Asparagine activase 1
Gene namesi
Name:mycA
OrganismiBacillus subtilis
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 39713971Mycosubtilin synthase subunit A
PRO_0000360848Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei613 – 6131O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residuei1324 – 13241O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residuei1759 – 17591N6-(pyridoxal phosphate)lysine By similarity
Modified residuei2440 – 24401O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residuei3477 – 34771O-(pantetheine 4'-phosphoryl)serine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9R9J1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini583 – 65068Acyl carrier 1
Add
BLAST
Domaini1292 – 136170Acyl carrier 2
Add
BLAST
Domaini2410 – 247768Acyl carrier 3
Add
BLAST
Domaini3447 – 351468Acyl carrier 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 479320Acyl-CoA ligase
Add
BLAST
Regioni672 – 1095424Beta-ketoacyl synthase
Add
BLAST
Regioni1529 – 1856328GSA-AT
Add
BLAST
Regioni1938 – 2240303Condensation 1
Add
BLAST
Regioni2492 – 2781290Condensation 2
Add
BLAST
Regioni2937 – 3823887Domain 1 (asparagine-activating)
Add
BLAST
Regioni2967 – 3364398Adenylation 1
Add
BLAST
Regioni3529 – 3818290Condensation 3
Add
BLAST

Sequence similaritiesi

Contains 4 acyl carrier domains.

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 4 hits.
3.40.47.10. 2 hits.
3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR005814. Aminotrans_3.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020806. PKS_PP-bd.
IPR006162. PPantetheine_attach_site.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00202. Aminotran_3. 1 hit.
PF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 3 hits.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF00550. PP-binding. 4 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 4 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 4 hits.
SSF53383. SSF53383. 1 hit.
SSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
PS50075. ACP_DOMAIN. 4 hits.
PS00455. AMP_BINDING. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R9J1-1 [UniParc]FASTAAdd to Basket

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MYTSQFQTLV DVIRNRSNIS DRGIRFIESD KIETFVSYRQ LFDEAQGFLG     50
YLQHIGIQPK QEIVFQIQEN KSFVVAFWAC LLGGMIPVPV SIGEDNDHKL 100
KVWRIWNILN NPFLLASETV LDKMKKFAAD HDLQDFHHQL IEKSDIIQDR 150
IYDHPASQYE PEADELAFIQ FSSGSTGDPK GVMLTHHNLI HNTCAIRNAL 200
AIDLKDTLLS WMPLTHDMGL IACHLVPALA GINQNLMPTE LFIRRPILWM 250
KKAHEHKASI LSSPNFGYNY FLKFLKDNKS YDWDLSHIRV IANGAEPILP 300
ELCDEFLTRC AAFNMKRSAI LNVYGLAEAS VGATFSNIGE RFVPVYLHRD 350
HLNLGERAVE VSKEDQNCAS FVEVGKPIDY CQIRICNEAN EGLEDGFIGH 400
IQIKGENVTQ GYYNNPESTN RALTPDGWVK TGDLGFIRKG NLVVTGREKD 450
IIFVNGKNVY PHDIERVAIE LEDIDLGRVA ACGVYDQETR SREIVLFAVY 500
KKSADRFAPL VKDIKKHLYQ RGGWSIKEIL PIRKLPKTTS GKVKRYELAE 550
QYESGKFALE STKIKEFLEG HSTEPVQTPI HEIETALLSI FSEVMDGKKI 600
HLNDHYFDMG ATSLQLSQIA ERIEQKFGCE LTVADLFTYP SIADLAAFLV 650
ENHSEIKQTD TAKPSRSSSK DIAIIGMSLN VPGASNKSDF WHLLENGEHG 700
IREYPAPRVK DAIDYLRSIK SERNEKQFVR GGYLDEIDRF DYSFFGLAPK 750
TAKFMDPNQR LFLQSAWHAI EDAGYAGDTI SGSQLGVYVG YSKVGYDYER 800
LLSANYPEEL HHYIVGNLPS VLASRIAYFL NLKGPAVTVD TACSSSLVAV 850
HMACKALLTG DCEMALAGGI RTSLLPMRIG LDMESSDGLT KTFSKDSDGT 900
GSGEGVAAVL LKPLQAAIRD GDHIYGVIKG SAINQDGTTV GITAPSPAAQ 950
TEVIEMAWKD AGIAPETLSF IEAHGTGTKL GDPVEFNGLC KAFEKVTEKK 1000
QFCAIGSVKA NIGHLFEAAG IVGLIKSALM LNHKKIPPLA HFNKPNPLIP 1050
FHSSPFYVNQ EVMDFTPEDR PLRGGISSFG FSGTNAHVVL EEYTPESEYA 1100
PEDGNDPHLF VLSAHTEASL YELTHQYRQY ISDDSQSSLR SICYTASTGR 1150
AHLDYCLAMI VSSNQELIDK LTSLIQGERN LPQVHFGYKN IKEMQPAEKD 1200
NLSKQISDLM QHRPCTKDER ITWLNRIAEL YVQRAVIDWR AVYSNEVVQK 1250
TPLPLYPFER NRCWVEAVYE SAKERKEKGE VALDINHTKT HIESFLKTVI 1300
SNASGIRADE IDSNAHFIGF GLDSIMLTQV KKAIADEFNV DIPMERFFDT 1350
MNNIESVVDY LAENVPSAAS TPPQESVTAQ EELVISGAQP ELEHQEHMLD 1400
KIIASQNQLI QQTLQAQLDS FNLLRNNSHF VSKESEISQD KTSLSPKSVT 1450
AKKNSAQEAK PYIPFQRQTL NEQVNYTPQQ RQYLESFIEK YVDKTKGSKQ 1500
YTDETRFAHA NNRNLSSFRS YWKEMVYPII AERSDGSRMW DIDGNEYIDI 1550
TMGFGVNLFG HHPSFITQTV VDSTHSALPP LGPMSNVAGE VADRIRACTG 1600
VERVAFYNSG TEAVMVALRL ARAATGRTKV VVFAGSYHGT FDGVLGVANT 1650
KGGAEPANPL APGIPQSFMN DLIILHYNHP DSLDVIRNLG NELAAVLVEP 1700
VQSRRPDLQP ESFLKELRAI TQQSGTALIM DEIITGFRIG LGGAQEWFDI 1750
QADLVTYGKI IGGGQPLGIV AGKAEFMNTI DGGTWQYGDD SYPTDEAKRT 1800
FVAGTFNTHP LTMRMSLAVL RYLQAEGETL YERLNQKTTY LVDQLNSYFE 1850
QSQVPIRMVQ FGSLFRFVSS VDNDLFFYHL NYKGVYVWEG RNCFLSTAHT 1900
SDDIAYIIQA VQETVKDLRR GGFIPEGPDS PNDGGHKEPE TYELSPEQKQ 1950
LAVVSQYGND ASAALNQSIM LKVKGAVQHT LLKQAVRNIV KRHDALRTVI 2000
HVDDEVQQVQ ARINVEIPII DFTGYPNEQR ESEVQKWLTE DAKRPFHFHE 2050
QKPLFRVHVL TSKQDEHLIV LTFHHIIADG WSIAVFVQEL ESTYAAIVQG 2100
SPLPSHEVVS FRQYLDWQQA QIENGHYEEG IRYWRQYLSE PIPQAILTSM 2150
SSSRYPHGYE GDRYTVTLDR PLSKAIKSLS IRMKNSVFAT ILGAFHLFLQ 2200
QLTKQAGLVI GIPTAGQLHM KQPMLVGNCV NMVPVKNTAS SESTLADYLG 2250
HMKENMDQVM RHQDVPMTLV ASQLPHDQMP DMRIIFNLDR PFRKLHFGQM 2300
EAELIAYPIK CISYDLFLNV TEFDQEYVLD FDFNTSVISS EIMNKWGTGF 2350
VNLLKKMVEG DSASLDSLKM FSKEDQHDLL ELYADHQLRI SSTLDHKGVR 2400
AVYEEPENET ELQIAQIWAE LLGLEKVGRS DHFLSLGGNS LKATLMLSKI 2450
QQTFNQKVSI GQFFSHQTVK ELANFIRGEK NVKYPPMKPV EQKAFYRTSP 2500
AQQRVYFLHQ MEPNQVSQNM FGQISIIGKY DEKALIASLQ QVMQRHEAFR 2550
TSFHIIDGEI VQQIAGELDF NVRVHSMDRE EFEAYADGYV KPFRLEQAPL 2600
VRAELIKVDN EQAELLIDMH HIISDGYSMS ILTNELFALY HGNPLPEIPF 2650
EYKDFAEWQN QLLIGEVMEQ QEEYWLEQFK QEVPILQLPA DGSRAMEWSS 2700
EGQRVTCSLQ SSLIRSLQEM AQQKGTTLYM VLLAAYNVLL HKYTGQEDIV 2750
VGTPVSGRNQ PNIESMIGIF IQTMGIRTKP QANKRFTDYL DEVKRQTLDA 2800
FENQDYPFDW LVEKVNVQRE TTGKSLFNTM FVYQNIEFQE IHQDGCTFRV 2850
KERNPGVSLY DLMLTIEDAE KQLDIHFDFN PNQFEQETIE QIIRHYTSLL 2900
DSLVKEPEKS LSSVPMLSDI ERHQLLMGCN DTETPFPHND TVCQWFETQA 2950
EQRPDDEAVI FGNERCTYGQ LNERVNQLAR TLRTKGVQAD QFVAIICPHR 3000
IELIVGILAV LKAGGAYVPI DPEYPEDRIQ YMLKDSEAKI VLAQLDLHKH 3050
LTFDADVVLL DEESSYHEDR SNLEPTCGAN DLAYMIYTSG STGNPKGVLI 3100
EHRGLANYIE WAKEVYVNDE KTNFPLYSSI SFDLTVTSIF TPLVTGNTII 3150
VFDGEDKSAV LSTIMQDPRI DIIKLTPAHL HVLKEMKIAD GTTIRKMIVG 3200
GENLSTRLAQ SVSEQFKGQL DIFNEYGPTE AVVGCMIYRY DTKRDRREFV 3250
PIGSPAANTS IYVLDASMNL VPVGVPGEMY IGGAGVARGY WNRPDLTAEK 3300
FVHNPFAPGT IMYKTGDLAK RLRDGNLIYL GRIDEQVKIR GHRIELGEVE 3350
AAMHKVEAVQ KAVVLAREEE DGLQQLCAYY VSNKPITIAE IREQLSLELP 3400
DYMVPSHYIQ LEQLPLTSNG KINRKALPAP EVSLEQIAEY VPPGNEVESK 3450
LAVLWQEMLG IHRVGIKHNF FDLGGNSIRA TALAARIHKE LDVNLSVKDI 3500
FKFPTIEQLA NMALRMEKIR YVSIPSAQKI SYYPVSSAQK RMYLLSHTEG 3550
GELTYNMTGA MSVEGAIDLE RLTAAFQKLI ERHEVLRTSF ELYEGEPAQR 3600
IHPSIEFTIE QIQAREEEVE DHVLDFIKSF DLAKPPLMRV GLIELTPEKH 3650
VLLVDMHHII SDGVSMNILM KDLNQFYKGI EPDPLPIQYK DYAVWQQTEA 3700
QRQNIKKQEA YWLNRFHDEI PVLDMPTDYE RPAIRDYEGE SFEFLIPIEL 3750
KQRLSQMEEA TGTTLYMILM AAYTILLSKY SGQEDIVVGT PVSGRSHMDV 3800
ESVVGMFVNT LVIRNHPAGR KIFEDYLNEV KENMLNAYQN QDYPLEELIQ 3850
HVHLLKDSSR NPLFDTMFVL QNLDQVELNL DSLRFTPYKL HHTVAKFDLT 3900
LSIQTDQDKH HGLFEYSKKL FKKSRIEALS KDYLHILSVI SQQPSIQIEH 3950
IELSGSTAED DNLIHSIELN F 3971
Length:3,971
Mass (Da):449,268
Last modified:May 1, 2000 - v1
Checksum:iC8BF27D87F10065B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184956 Genomic DNA. Translation: AAF08795.1.
PIRiT44806.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184956 Genomic DNA. Translation: AAF08795.1 .
PIRi T44806.

3D structure databases

ProteinModelPortali Q9R9J1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.1200.10. 4 hits.
3.40.47.10. 2 hits.
3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProi IPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR005814. Aminotrans_3.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020806. PKS_PP-bd.
IPR006162. PPantetheine_attach_site.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00202. Aminotran_3. 1 hit.
PF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 3 hits.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF00550. PP-binding. 4 hits.
[Graphical view ]
SMARTi SM00823. PKS_PP. 4 hits.
[Graphical view ]
SUPFAMi SSF47336. SSF47336. 4 hits.
SSF53383. SSF53383. 1 hit.
SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
PS50075. ACP_DOMAIN. 4 hits.
PS00455. AMP_BINDING. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a multifunctional hybrid between a peptide synthetase, an amino transferase, and a fatty acid synthase."
    Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W., Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F., Vater J.
    Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6633 / PCI 219 / NRS 231.
  2. "Characterization of a new tailoring domain in polyketide biogenesis: the amine transferase domain of MycA in the mycosubtilin gene cluster."
    Aron Z.D., Dorrestein P.C., Blackhall J.R., Kelleher N.L., Walsh C.T.
    J. Am. Chem. Soc. 127:14986-14987(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR OF AMINOTRANSFERASE DOMAIN.

Entry informationi

Entry nameiMYCA_BACIU
AccessioniPrimary (citable) accession number: Q9R9J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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