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 03-APR-2013, entry version 67.
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 HSSP; O30409; 1DNY.
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; 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; 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; ACP_like; 4.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
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; Pyridoxal phosphate; Repeat; 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
//
