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Database: UniProt
Entry: Q9R9J1
LinkDB: Q9R9J1
Original site: Q9R9J1 
ID   MYCA_BACIU              Reviewed;        3971 AA.
AC   Q9R9J1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   19-FEB-2014, entry version 71.
DE   RecName: Full=Mycosubtilin synthase subunit A;
DE            EC=2.3.1.-;
DE   Includes:
DE     RecName: Full=Glutamate-1-semialdehyde aminotransferase;
DE              Short=GSA-AT;
DE   Includes:
DE     RecName: Full=ATP-dependent asparagine adenylase 1;
DE              Short=AsnA 1;
DE     AltName: Full=Asparagine activase 1;
GN   Name=mycA;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=10557314; DOI=10.1073/pnas.96.23.13294;
RA   Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H.,
RA   Saenger W., Bernhard F., Reinhardt R., Schmidt M., Ullrich C.,
RA   Stein T., Leenders F., Vater J.;
RT   "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a
RT   multifunctional hybrid between a peptide synthetase, an amino
RT   transferase, and a fatty acid synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999).
RN   [2]
RP   FUNCTION, AND COFACTOR OF AMINOTRANSFERASE DOMAIN.
RX   PubMed=16248612; DOI=10.1021/ja055247g;
RA   Aron Z.D., Dorrestein P.C., Blackhall J.R., Kelleher N.L., Walsh C.T.;
RT   "Characterization of a new tailoring domain in polyketide biogenesis:
RT   the amine transferase domain of MycA in the mycosubtilin gene
RT   cluster.";
RL   J. Am. Chem. Soc. 127:14986-14987(2005).
CC   -!- FUNCTION: This protein is a multifunctional enzyme, able to
CC       activate a long chain fatty acid and link it with the amino acid
CC       Asn as part of the synthesis of mycosubtilin. The activation sites
CC       consist of individual domains.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- COFACTOR: Binds 2 phosphopantetheines covalently (Potential).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -!- SIMILARITY: Contains 4 acyl carrier domains.
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DR   EMBL; AF184956; AAF08795.1; -; Genomic_DNA.
DR   PIR; T44806; T44806.
DR   ProteinModelPortal; Q9R9J1; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 4.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 4.
DR   SMART; SM00823; PKS_PP; 4.
DR   SUPFAM; SSF47336; SSF47336; 4.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 4.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW   Phosphopantetheine; Phosphoprotein; Pyridoxal phosphate; Repeat;
KW   Transferase.
FT   CHAIN         1   3971       Mycosubtilin synthase subunit A.
FT                                /FTId=PRO_0000360848.
FT   DOMAIN      583    650       Acyl carrier 1.
FT   DOMAIN     1292   1361       Acyl carrier 2.
FT   DOMAIN     2410   2477       Acyl carrier 3.
FT   DOMAIN     3447   3514       Acyl carrier 4.
FT   REGION      160    479       Acyl-CoA ligase.
FT   REGION      672   1095       Beta-ketoacyl synthase.
FT   REGION     1529   1856       GSA-AT.
FT   REGION     1938   2240       Condensation 1.
FT   REGION     2492   2781       Condensation 2.
FT   REGION     2937   3823       Domain 1 (asparagine-activating).
FT   REGION     2967   3364       Adenylation 1.
FT   REGION     3529   3818       Condensation 3.
FT   ACT_SITE    843    843       For beta-ketoacyl synthase activity (By
FT                                similarity).
FT   MOD_RES     613    613       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    1324   1324       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    1759   1759       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   MOD_RES    2440   2440       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    3477   3477       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
SQ   SEQUENCE   3971 AA;  449268 MW;  C8BF27D87F10065B CRC64;
     MYTSQFQTLV DVIRNRSNIS DRGIRFIESD KIETFVSYRQ LFDEAQGFLG YLQHIGIQPK
     QEIVFQIQEN KSFVVAFWAC LLGGMIPVPV SIGEDNDHKL KVWRIWNILN NPFLLASETV
     LDKMKKFAAD HDLQDFHHQL IEKSDIIQDR IYDHPASQYE PEADELAFIQ FSSGSTGDPK
     GVMLTHHNLI HNTCAIRNAL AIDLKDTLLS WMPLTHDMGL IACHLVPALA GINQNLMPTE
     LFIRRPILWM KKAHEHKASI LSSPNFGYNY FLKFLKDNKS YDWDLSHIRV IANGAEPILP
     ELCDEFLTRC AAFNMKRSAI LNVYGLAEAS VGATFSNIGE RFVPVYLHRD HLNLGERAVE
     VSKEDQNCAS FVEVGKPIDY CQIRICNEAN EGLEDGFIGH IQIKGENVTQ GYYNNPESTN
     RALTPDGWVK TGDLGFIRKG NLVVTGREKD IIFVNGKNVY PHDIERVAIE LEDIDLGRVA
     ACGVYDQETR SREIVLFAVY KKSADRFAPL VKDIKKHLYQ RGGWSIKEIL PIRKLPKTTS
     GKVKRYELAE QYESGKFALE STKIKEFLEG HSTEPVQTPI HEIETALLSI FSEVMDGKKI
     HLNDHYFDMG ATSLQLSQIA ERIEQKFGCE LTVADLFTYP SIADLAAFLV ENHSEIKQTD
     TAKPSRSSSK DIAIIGMSLN VPGASNKSDF WHLLENGEHG IREYPAPRVK DAIDYLRSIK
     SERNEKQFVR GGYLDEIDRF DYSFFGLAPK TAKFMDPNQR LFLQSAWHAI EDAGYAGDTI
     SGSQLGVYVG YSKVGYDYER LLSANYPEEL HHYIVGNLPS VLASRIAYFL NLKGPAVTVD
     TACSSSLVAV HMACKALLTG DCEMALAGGI RTSLLPMRIG LDMESSDGLT KTFSKDSDGT
     GSGEGVAAVL LKPLQAAIRD GDHIYGVIKG SAINQDGTTV GITAPSPAAQ TEVIEMAWKD
     AGIAPETLSF IEAHGTGTKL GDPVEFNGLC KAFEKVTEKK QFCAIGSVKA NIGHLFEAAG
     IVGLIKSALM LNHKKIPPLA HFNKPNPLIP FHSSPFYVNQ EVMDFTPEDR PLRGGISSFG
     FSGTNAHVVL EEYTPESEYA PEDGNDPHLF VLSAHTEASL YELTHQYRQY ISDDSQSSLR
     SICYTASTGR AHLDYCLAMI VSSNQELIDK LTSLIQGERN LPQVHFGYKN IKEMQPAEKD
     NLSKQISDLM QHRPCTKDER ITWLNRIAEL YVQRAVIDWR AVYSNEVVQK TPLPLYPFER
     NRCWVEAVYE SAKERKEKGE VALDINHTKT HIESFLKTVI SNASGIRADE IDSNAHFIGF
     GLDSIMLTQV KKAIADEFNV DIPMERFFDT MNNIESVVDY LAENVPSAAS TPPQESVTAQ
     EELVISGAQP ELEHQEHMLD KIIASQNQLI QQTLQAQLDS FNLLRNNSHF VSKESEISQD
     KTSLSPKSVT AKKNSAQEAK PYIPFQRQTL NEQVNYTPQQ RQYLESFIEK YVDKTKGSKQ
     YTDETRFAHA NNRNLSSFRS YWKEMVYPII AERSDGSRMW DIDGNEYIDI TMGFGVNLFG
     HHPSFITQTV VDSTHSALPP LGPMSNVAGE VADRIRACTG VERVAFYNSG TEAVMVALRL
     ARAATGRTKV VVFAGSYHGT FDGVLGVANT KGGAEPANPL APGIPQSFMN DLIILHYNHP
     DSLDVIRNLG NELAAVLVEP VQSRRPDLQP ESFLKELRAI TQQSGTALIM DEIITGFRIG
     LGGAQEWFDI QADLVTYGKI IGGGQPLGIV AGKAEFMNTI DGGTWQYGDD SYPTDEAKRT
     FVAGTFNTHP LTMRMSLAVL RYLQAEGETL YERLNQKTTY LVDQLNSYFE QSQVPIRMVQ
     FGSLFRFVSS VDNDLFFYHL NYKGVYVWEG RNCFLSTAHT SDDIAYIIQA VQETVKDLRR
     GGFIPEGPDS PNDGGHKEPE TYELSPEQKQ LAVVSQYGND ASAALNQSIM LKVKGAVQHT
     LLKQAVRNIV KRHDALRTVI HVDDEVQQVQ ARINVEIPII DFTGYPNEQR ESEVQKWLTE
     DAKRPFHFHE QKPLFRVHVL TSKQDEHLIV LTFHHIIADG WSIAVFVQEL ESTYAAIVQG
     SPLPSHEVVS FRQYLDWQQA QIENGHYEEG IRYWRQYLSE PIPQAILTSM SSSRYPHGYE
     GDRYTVTLDR PLSKAIKSLS IRMKNSVFAT ILGAFHLFLQ QLTKQAGLVI GIPTAGQLHM
     KQPMLVGNCV NMVPVKNTAS SESTLADYLG HMKENMDQVM RHQDVPMTLV ASQLPHDQMP
     DMRIIFNLDR PFRKLHFGQM EAELIAYPIK CISYDLFLNV TEFDQEYVLD FDFNTSVISS
     EIMNKWGTGF VNLLKKMVEG DSASLDSLKM FSKEDQHDLL ELYADHQLRI SSTLDHKGVR
     AVYEEPENET ELQIAQIWAE LLGLEKVGRS DHFLSLGGNS LKATLMLSKI QQTFNQKVSI
     GQFFSHQTVK ELANFIRGEK NVKYPPMKPV EQKAFYRTSP AQQRVYFLHQ MEPNQVSQNM
     FGQISIIGKY DEKALIASLQ QVMQRHEAFR TSFHIIDGEI VQQIAGELDF NVRVHSMDRE
     EFEAYADGYV KPFRLEQAPL VRAELIKVDN EQAELLIDMH HIISDGYSMS ILTNELFALY
     HGNPLPEIPF EYKDFAEWQN QLLIGEVMEQ QEEYWLEQFK QEVPILQLPA DGSRAMEWSS
     EGQRVTCSLQ SSLIRSLQEM AQQKGTTLYM VLLAAYNVLL HKYTGQEDIV VGTPVSGRNQ
     PNIESMIGIF IQTMGIRTKP QANKRFTDYL DEVKRQTLDA FENQDYPFDW LVEKVNVQRE
     TTGKSLFNTM FVYQNIEFQE IHQDGCTFRV KERNPGVSLY DLMLTIEDAE KQLDIHFDFN
     PNQFEQETIE QIIRHYTSLL DSLVKEPEKS LSSVPMLSDI ERHQLLMGCN DTETPFPHND
     TVCQWFETQA EQRPDDEAVI FGNERCTYGQ LNERVNQLAR TLRTKGVQAD QFVAIICPHR
     IELIVGILAV LKAGGAYVPI DPEYPEDRIQ YMLKDSEAKI VLAQLDLHKH LTFDADVVLL
     DEESSYHEDR SNLEPTCGAN DLAYMIYTSG STGNPKGVLI EHRGLANYIE WAKEVYVNDE
     KTNFPLYSSI SFDLTVTSIF TPLVTGNTII VFDGEDKSAV LSTIMQDPRI DIIKLTPAHL
     HVLKEMKIAD GTTIRKMIVG GENLSTRLAQ SVSEQFKGQL DIFNEYGPTE AVVGCMIYRY
     DTKRDRREFV PIGSPAANTS IYVLDASMNL VPVGVPGEMY IGGAGVARGY WNRPDLTAEK
     FVHNPFAPGT IMYKTGDLAK RLRDGNLIYL GRIDEQVKIR GHRIELGEVE AAMHKVEAVQ
     KAVVLAREEE DGLQQLCAYY VSNKPITIAE IREQLSLELP DYMVPSHYIQ LEQLPLTSNG
     KINRKALPAP EVSLEQIAEY VPPGNEVESK LAVLWQEMLG IHRVGIKHNF FDLGGNSIRA
     TALAARIHKE LDVNLSVKDI FKFPTIEQLA NMALRMEKIR YVSIPSAQKI SYYPVSSAQK
     RMYLLSHTEG GELTYNMTGA MSVEGAIDLE RLTAAFQKLI ERHEVLRTSF ELYEGEPAQR
     IHPSIEFTIE QIQAREEEVE DHVLDFIKSF DLAKPPLMRV GLIELTPEKH VLLVDMHHII
     SDGVSMNILM KDLNQFYKGI EPDPLPIQYK DYAVWQQTEA QRQNIKKQEA YWLNRFHDEI
     PVLDMPTDYE RPAIRDYEGE SFEFLIPIEL KQRLSQMEEA TGTTLYMILM AAYTILLSKY
     SGQEDIVVGT PVSGRSHMDV ESVVGMFVNT LVIRNHPAGR KIFEDYLNEV KENMLNAYQN
     QDYPLEELIQ HVHLLKDSSR NPLFDTMFVL QNLDQVELNL DSLRFTPYKL HHTVAKFDLT
     LSIQTDQDKH HGLFEYSKKL FKKSRIEALS KDYLHILSVI SQQPSIQIEH IELSGSTAED
     DNLIHSIELN F
//
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