Q9R9J1 (MYCA_BACIU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mycosubtilin synthase subunit A
EC=2.3.1.-

Including the following 2 domains:

1. Glutamate-1-semialdehyde aminotransferase
   Short name=GSA-AT
2. ATP-dependent asparagine adenylase 1
   Short name=AsnA 1
   Alternative name(s):
   Asparagine activase 1

Gene names

Name:

mycA

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group

Protein attributes

Sequence length	3971 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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. Ref.2
Cofactor	Pyridoxal phosphate. Ref.2 Binds 2 phosphopantetheines covalently Potential. Ref.2
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Contains 4 acyl carrier domains.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Domain	Repeat
Ligand	Phosphopantetheine Pyridoxal phosphate
Molecular function	Ligase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological_process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW phosphopantetheine binding Inferred from electronic annotation. Source: InterPro pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transaminase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3971	3971	Mycosubtilin synthase subunit A		PRO_0000360848
Regions
	Domain	583 – 650	68	Acyl carrier 1
	Domain	1292 – 1361	70	Acyl carrier 2
	Domain	2410 – 2477	68	Acyl carrier 3
	Domain	3447 – 3514	68	Acyl carrier 4
	Region	160 – 479	320	Acyl-CoA ligase
	Region	672 – 1095	424	Beta-ketoacyl synthase
	Region	1529 – 1856	328	GSA-AT
	Region	1938 – 2240	303	Condensation 1
	Region	2492 – 2781	290	Condensation 2
	Region	2937 – 3823	887	Domain 1 (asparagine-activating)
	Region	2967 – 3364	398	Adenylation 1
	Region	3529 – 3818	290	Condensation 3
Sites
	Active site	843	1	For beta-ketoacyl synthase activity By similarity
Amino acid modifications
	Modified residue	613	1	O-(pantetheine 4'-phosphoryl)serine By similarity
	Modified residue	1324	1	O-(pantetheine 4'-phosphoryl)serine By similarity
	Modified residue	1759	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	2440	1	O-(pantetheine 4'-phosphoryl)serine By similarity
	Modified residue	3477	1	O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9R9J1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C8BF27D87F10065B	FASTA	3,971	449,268
	10 20 30 40 50 60 MYTSQFQTLV DVIRNRSNIS DRGIRFIESD KIETFVSYRQ LFDEAQGFLG YLQHIGIQPK 70 80 90 100 110 120 QEIVFQIQEN KSFVVAFWAC LLGGMIPVPV SIGEDNDHKL KVWRIWNILN NPFLLASETV 130 140 150 160 170 180 LDKMKKFAAD HDLQDFHHQL IEKSDIIQDR IYDHPASQYE PEADELAFIQ FSSGSTGDPK 190 200 210 220 230 240 GVMLTHHNLI HNTCAIRNAL AIDLKDTLLS WMPLTHDMGL IACHLVPALA GINQNLMPTE 250 260 270 280 290 300 LFIRRPILWM KKAHEHKASI LSSPNFGYNY FLKFLKDNKS YDWDLSHIRV IANGAEPILP 310 320 330 340 350 360 ELCDEFLTRC AAFNMKRSAI LNVYGLAEAS VGATFSNIGE RFVPVYLHRD HLNLGERAVE 370 380 390 400 410 420 VSKEDQNCAS FVEVGKPIDY CQIRICNEAN EGLEDGFIGH IQIKGENVTQ GYYNNPESTN 430 440 450 460 470 480 RALTPDGWVK TGDLGFIRKG NLVVTGREKD IIFVNGKNVY PHDIERVAIE LEDIDLGRVA 490 500 510 520 530 540 ACGVYDQETR SREIVLFAVY KKSADRFAPL VKDIKKHLYQ RGGWSIKEIL PIRKLPKTTS 550 560 570 580 590 600 GKVKRYELAE QYESGKFALE STKIKEFLEG HSTEPVQTPI HEIETALLSI FSEVMDGKKI 610 620 630 640 650 660 HLNDHYFDMG ATSLQLSQIA ERIEQKFGCE LTVADLFTYP SIADLAAFLV ENHSEIKQTD 670 680 690 700 710 720 TAKPSRSSSK DIAIIGMSLN VPGASNKSDF WHLLENGEHG IREYPAPRVK DAIDYLRSIK 730 740 750 760 770 780 SERNEKQFVR GGYLDEIDRF DYSFFGLAPK TAKFMDPNQR LFLQSAWHAI EDAGYAGDTI 790 800 810 820 830 840 SGSQLGVYVG YSKVGYDYER LLSANYPEEL HHYIVGNLPS VLASRIAYFL NLKGPAVTVD 850 860 870 880 890 900 TACSSSLVAV HMACKALLTG DCEMALAGGI RTSLLPMRIG LDMESSDGLT KTFSKDSDGT 910 920 930 940 950 960 GSGEGVAAVL LKPLQAAIRD GDHIYGVIKG SAINQDGTTV GITAPSPAAQ TEVIEMAWKD 970 980 990 1000 1010 1020 AGIAPETLSF IEAHGTGTKL GDPVEFNGLC KAFEKVTEKK QFCAIGSVKA NIGHLFEAAG 1030 1040 1050 1060 1070 1080 IVGLIKSALM LNHKKIPPLA HFNKPNPLIP FHSSPFYVNQ EVMDFTPEDR PLRGGISSFG 1090 1100 1110 1120 1130 1140 FSGTNAHVVL EEYTPESEYA PEDGNDPHLF VLSAHTEASL YELTHQYRQY ISDDSQSSLR 1150 1160 1170 1180 1190 1200 SICYTASTGR AHLDYCLAMI VSSNQELIDK LTSLIQGERN LPQVHFGYKN IKEMQPAEKD 1210 1220 1230 1240 1250 1260 NLSKQISDLM QHRPCTKDER ITWLNRIAEL YVQRAVIDWR AVYSNEVVQK TPLPLYPFER 1270 1280 1290 1300 1310 1320 NRCWVEAVYE SAKERKEKGE VALDINHTKT HIESFLKTVI SNASGIRADE IDSNAHFIGF 1330 1340 1350 1360 1370 1380 GLDSIMLTQV KKAIADEFNV DIPMERFFDT MNNIESVVDY LAENVPSAAS TPPQESVTAQ 1390 1400 1410 1420 1430 1440 EELVISGAQP ELEHQEHMLD KIIASQNQLI QQTLQAQLDS FNLLRNNSHF VSKESEISQD 1450 1460 1470 1480 1490 1500 KTSLSPKSVT AKKNSAQEAK PYIPFQRQTL NEQVNYTPQQ RQYLESFIEK YVDKTKGSKQ 1510 1520 1530 1540 1550 1560 YTDETRFAHA NNRNLSSFRS YWKEMVYPII AERSDGSRMW DIDGNEYIDI TMGFGVNLFG 1570 1580 1590 1600 1610 1620 HHPSFITQTV VDSTHSALPP LGPMSNVAGE VADRIRACTG VERVAFYNSG TEAVMVALRL 1630 1640 1650 1660 1670 1680 ARAATGRTKV VVFAGSYHGT FDGVLGVANT KGGAEPANPL APGIPQSFMN DLIILHYNHP 1690 1700 1710 1720 1730 1740 DSLDVIRNLG NELAAVLVEP VQSRRPDLQP ESFLKELRAI TQQSGTALIM DEIITGFRIG 1750 1760 1770 1780 1790 1800 LGGAQEWFDI QADLVTYGKI IGGGQPLGIV AGKAEFMNTI DGGTWQYGDD SYPTDEAKRT 1810 1820 1830 1840 1850 1860 FVAGTFNTHP LTMRMSLAVL RYLQAEGETL YERLNQKTTY LVDQLNSYFE QSQVPIRMVQ 1870 1880 1890 1900 1910 1920 FGSLFRFVSS VDNDLFFYHL NYKGVYVWEG RNCFLSTAHT SDDIAYIIQA VQETVKDLRR 1930 1940 1950 1960 1970 1980 GGFIPEGPDS PNDGGHKEPE TYELSPEQKQ LAVVSQYGND ASAALNQSIM LKVKGAVQHT 1990 2000 2010 2020 2030 2040 LLKQAVRNIV KRHDALRTVI HVDDEVQQVQ ARINVEIPII DFTGYPNEQR ESEVQKWLTE 2050 2060 2070 2080 2090 2100 DAKRPFHFHE QKPLFRVHVL TSKQDEHLIV LTFHHIIADG WSIAVFVQEL ESTYAAIVQG 2110 2120 2130 2140 2150 2160 SPLPSHEVVS FRQYLDWQQA QIENGHYEEG IRYWRQYLSE PIPQAILTSM SSSRYPHGYE 2170 2180 2190 2200 2210 2220 GDRYTVTLDR PLSKAIKSLS IRMKNSVFAT ILGAFHLFLQ QLTKQAGLVI GIPTAGQLHM 2230 2240 2250 2260 2270 2280 KQPMLVGNCV NMVPVKNTAS SESTLADYLG HMKENMDQVM RHQDVPMTLV ASQLPHDQMP 2290 2300 2310 2320 2330 2340 DMRIIFNLDR PFRKLHFGQM EAELIAYPIK CISYDLFLNV TEFDQEYVLD FDFNTSVISS 2350 2360 2370 2380 2390 2400 EIMNKWGTGF VNLLKKMVEG DSASLDSLKM FSKEDQHDLL ELYADHQLRI SSTLDHKGVR 2410 2420 2430 2440 2450 2460 AVYEEPENET ELQIAQIWAE LLGLEKVGRS DHFLSLGGNS LKATLMLSKI QQTFNQKVSI 2470 2480 2490 2500 2510 2520 GQFFSHQTVK ELANFIRGEK NVKYPPMKPV EQKAFYRTSP AQQRVYFLHQ MEPNQVSQNM 2530 2540 2550 2560 2570 2580 FGQISIIGKY DEKALIASLQ QVMQRHEAFR TSFHIIDGEI VQQIAGELDF NVRVHSMDRE 2590 2600 2610 2620 2630 2640 EFEAYADGYV KPFRLEQAPL VRAELIKVDN EQAELLIDMH HIISDGYSMS ILTNELFALY 2650 2660 2670 2680 2690 2700 HGNPLPEIPF EYKDFAEWQN QLLIGEVMEQ QEEYWLEQFK QEVPILQLPA DGSRAMEWSS 2710 2720 2730 2740 2750 2760 EGQRVTCSLQ SSLIRSLQEM AQQKGTTLYM VLLAAYNVLL HKYTGQEDIV VGTPVSGRNQ 2770 2780 2790 2800 2810 2820 PNIESMIGIF IQTMGIRTKP QANKRFTDYL DEVKRQTLDA FENQDYPFDW LVEKVNVQRE 2830 2840 2850 2860 2870 2880 TTGKSLFNTM FVYQNIEFQE IHQDGCTFRV KERNPGVSLY DLMLTIEDAE KQLDIHFDFN 2890 2900 2910 2920 2930 2940 PNQFEQETIE QIIRHYTSLL DSLVKEPEKS LSSVPMLSDI ERHQLLMGCN DTETPFPHND 2950 2960 2970 2980 2990 3000 TVCQWFETQA EQRPDDEAVI FGNERCTYGQ LNERVNQLAR TLRTKGVQAD QFVAIICPHR 3010 3020 3030 3040 3050 3060 IELIVGILAV LKAGGAYVPI DPEYPEDRIQ YMLKDSEAKI VLAQLDLHKH LTFDADVVLL 3070 3080 3090 3100 3110 3120 DEESSYHEDR SNLEPTCGAN DLAYMIYTSG STGNPKGVLI EHRGLANYIE WAKEVYVNDE 3130 3140 3150 3160 3170 3180 KTNFPLYSSI SFDLTVTSIF TPLVTGNTII VFDGEDKSAV LSTIMQDPRI DIIKLTPAHL 3190 3200 3210 3220 3230 3240 HVLKEMKIAD GTTIRKMIVG GENLSTRLAQ SVSEQFKGQL DIFNEYGPTE AVVGCMIYRY 3250 3260 3270 3280 3290 3300 DTKRDRREFV PIGSPAANTS IYVLDASMNL VPVGVPGEMY IGGAGVARGY WNRPDLTAEK 3310 3320 3330 3340 3350 3360 FVHNPFAPGT IMYKTGDLAK RLRDGNLIYL GRIDEQVKIR GHRIELGEVE AAMHKVEAVQ 3370 3380 3390 3400 3410 3420 KAVVLAREEE DGLQQLCAYY VSNKPITIAE IREQLSLELP DYMVPSHYIQ LEQLPLTSNG 3430 3440 3450 3460 3470 3480 KINRKALPAP EVSLEQIAEY VPPGNEVESK LAVLWQEMLG IHRVGIKHNF FDLGGNSIRA 3490 3500 3510 3520 3530 3540 TALAARIHKE LDVNLSVKDI FKFPTIEQLA NMALRMEKIR YVSIPSAQKI SYYPVSSAQK 3550 3560 3570 3580 3590 3600 RMYLLSHTEG GELTYNMTGA MSVEGAIDLE RLTAAFQKLI ERHEVLRTSF ELYEGEPAQR 3610 3620 3630 3640 3650 3660 IHPSIEFTIE QIQAREEEVE DHVLDFIKSF DLAKPPLMRV GLIELTPEKH VLLVDMHHII 3670 3680 3690 3700 3710 3720 SDGVSMNILM KDLNQFYKGI EPDPLPIQYK DYAVWQQTEA QRQNIKKQEA YWLNRFHDEI 3730 3740 3750 3760 3770 3780 PVLDMPTDYE RPAIRDYEGE SFEFLIPIEL KQRLSQMEEA TGTTLYMILM AAYTILLSKY 3790 3800 3810 3820 3830 3840 SGQEDIVVGT PVSGRSHMDV ESVVGMFVNT LVIRNHPAGR KIFEDYLNEV KENMLNAYQN 3850 3860 3870 3880 3890 3900 QDYPLEELIQ HVHLLKDSSR NPLFDTMFVL QNLDQVELNL DSLRFTPYKL HHTVAKFDLT 3910 3920 3930 3940 3950 3960 LSIQTDQDKH HGLFEYSKKL FKKSRIEALS KDYLHILSVI SQQPSIQIEH IELSGSTAED 3970 DNLIHSIELN F

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF184956 Genomic DNA. Translation: AAF08795.1.
PIR	T44806.
3D structure databases
ProteinModelPortal	Q9R9J1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.1200.10. 4 hits. 3.40.47.10. 2 hits. 3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
InterPro	IPR010071. AA_adenyl_domain. IPR009081. Acyl_carrier_prot-like. IPR005814. Aminotrans_3. 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]
Pfam	PF00202. Aminotran_3. 1 hit. PF00501. AMP-binding. 2 hits. PF00668. Condensation. 3 hits. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. PF00550. PP-binding. 4 hits. [Graphical view]
SMART	SM00823. PKS_PP. 4 hits. [Graphical view]
SUPFAM	SSF47336. ACP_like. 4 hits. SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. SSF53901. Thiolase-like. 1 hit.
TIGRFAMs	TIGR01733. AA-adenyl-dom. 1 hit.
PROSITE	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]
ProtoNet	Search...

Entry information

Entry name

MYCA_BACIU

Accession

Primary (citable) accession number: Q9R9J1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program