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Q9R9J1

- MYCA_BACIU

UniProt

Q9R9J1 - MYCA_BACIU

Protein

Mycosubtilin synthase subunit A

Gene

mycA

Organism
Bacillus subtilis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei843 – 8431For beta-ketoacyl synthase activityPROSITE-ProRule annotation

    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

    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 APRO_0000360848Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R9J1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    Sequence similaritiesi

    Contains 4 acyl carrier domains.PROSITE-ProRule annotation

    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: October 1, 2014
    This is version 72 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