MYCA_BACIU
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-AUG-2022, entry version 95.
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., Saenger W.,
RA Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F.,
RA Vater J.;
RT "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a
RT multifunctional hybrid between a peptide synthetase, an amino transferase,
RT 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: the
RT amine transferase domain of MycA in the mycosubtilin gene cluster.";
RL J. Am. Chem. Soc. 127:14986-14987(2005).
CC -!- FUNCTION: This protein is a multifunctional enzyme, able to activate a
CC long chain fatty acid and link it with the amino acid Asn as part of
CC the synthesis of mycosubtilin. The activation sites consist of
CC individual domains. {ECO:0000269|PubMed:16248612}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:16248612};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF184956; AAF08795.1; -; Genomic_DNA.
DR PIR; T44806; T44806.
DR PDB; 6KFM; X-ray; 1.70 A; A/B=1470-1930.
DR PDB; 6KFR; X-ray; 3.10 A; A/B=1470-1930.
DR PDB; 6KFU; X-ray; 2.20 A; A=1282-1370, A=1470-1930.
DR PDBsum; 6KFM; -.
DR PDBsum; 6KFR; -.
DR PDBsum; 6KFU; -.
DR SMR; Q9R9J1; -.
DR PRIDE; Q9R9J1; -.
DR SABIO-RK; Q9R9J1; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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 GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 1.10.1200.10; -; 4.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 3.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 4.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF47336; SSF47336; 4.
DR SUPFAM; SSF53383; SSF53383; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW Phosphopantetheine; Phosphoprotein; Pyridoxal phosphate; Repeat;
KW Transferase.
FT CHAIN 1..3971
FT /note="Mycosubtilin synthase subunit A"
FT /id="PRO_0000360848"
FT DOMAIN 578..653
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1290..1365
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2405..2480
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3442..3517
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 160..479
FT /note="Acyl-CoA ligase"
FT REGION 672..1095
FT /note="Beta-ketoacyl synthase"
FT REGION 1434..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1856
FT /note="GSA-AT"
FT REGION 1921..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1938..2240
FT /note="Condensation 1"
FT REGION 2492..2781
FT /note="Condensation 2"
FT REGION 2937..3823
FT /note="Domain 1 (asparagine-activating)"
FT REGION 2967..3364
FT /note="Adenylation 1"
FT REGION 3529..3818
FT /note="Condensation 3"
FT ACT_SITE 843
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 613
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1324
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1759
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 2440
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3477
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT HELIX 1288..1304
FT /evidence="ECO:0007829|PDB:6KFU"
FT HELIX 1308..1310
FT /evidence="ECO:0007829|PDB:6KFU"
FT STRAND 1313..1315
FT /evidence="ECO:0007829|PDB:6KFU"
FT HELIX 1317..1320
FT /evidence="ECO:0007829|PDB:6KFU"
FT HELIX 1324..1337
FT /evidence="ECO:0007829|PDB:6KFU"
FT HELIX 1344..1348
FT /evidence="ECO:0007829|PDB:6KFU"
FT HELIX 1354..1361
FT /evidence="ECO:0007829|PDB:6KFU"
FT HELIX 1478..1494
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1496..1505
FT /evidence="ECO:0007829|PDB:6KFM"
FT TURN 1506..1508
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1512..1515
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1520..1525
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1530..1536
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1538..1541
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1546..1551
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1552..1555
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1564..1575
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1581..1587
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1588..1599
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1602..1609
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1610..1625
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1629..1633
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1642..1644
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1658..1661
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1666..1669
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1672..1675
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1680..1689
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1690..1692
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1693..1698
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1711..1724
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1727..1731
FT /evidence="ECO:0007829|PDB:6KFM"
FT TURN 1733..1738
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1743..1748
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1753..1758
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1759..1762
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1768..1772
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1774..1781
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1787..1790
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1796..1798
FT /evidence="ECO:0007829|PDB:6KFM"
FT TURN 1805..1808
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1810..1826
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1828..1851
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1855..1861
FT /evidence="ECO:0007829|PDB:6KFM"
FT STRAND 1864..1871
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1873..1882
FT /evidence="ECO:0007829|PDB:6KFM"
FT HELIX 1901..1920
FT /evidence="ECO:0007829|PDB:6KFM"
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
