BTRJ_NIACI
ID BTRJ_NIACI Reviewed; 419 AA.
AC Q4H4E7;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=[Butirosin acyl-carrier protein]--L-glutamate ligase;
DE EC=6.2.1.39;
DE AltName: Full=Butirosin biosynthesis protein J;
GN Name=btrJ;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX PubMed=16156513; DOI=10.1038/ja.2005.47;
RA Kudo F., Numakura M., Tamegai H., Yamamoto H., Eguchi T., Kakinuma K.;
RT "Extended sequence and functional analysis of the butirosin biosynthetic
RT gene cluster in Bacillus circulans SANK 72073.";
RL J. Antibiot. 58:373-379(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RA Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Analysis and comparison of the biosynthetic gene clusters for the 2-
RT deoxystreptamine-containing aminoglycoside antibiotics ribostamycin,
RT neomycin, lividomycin, paromomycin and butirosin.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX PubMed=15975512; DOI=10.1016/j.chembiol.2005.04.010;
RA Li Y., Llewellyn N.M., Giri R., Huang F., Spencer J.B.;
RT "Biosynthesis of the unique amino acid side chain of butirosin: possible
RT protective-group chemistry in an acyl carrier protein-mediated pathway.";
RL Chem. Biol. 12:665-675(2005).
CC -!- FUNCTION: ATP-dependent ligase that catalyzes 2 steps in the
CC biosynthesis of the side chain of the aminoglycoside antibiotics in the
CC biosynthetic pathway of butirosin. Mediates the addition of one
CC molecule of L-glutamate to a dedicated acyl-carrier protein. Following
CC decarboxylation of the product by BtrK, adds a second L-glutamate
CC molecule. {ECO:0000269|PubMed:15975512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[BtrI ACP] + L-glutamate = ADP + gamma-L-glutamyl-
CC [BtrI ACP] + phosphate; Xref=Rhea:RHEA:53948, Rhea:RHEA-COMP:13741,
CC Rhea:RHEA-COMP:13742, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:64479, ChEBI:CHEBI:137996,
CC ChEBI:CHEBI:456216; EC=6.2.1.39;
CC Evidence={ECO:0000269|PubMed:15975512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoyl-[BtrI ACP] + ATP + L-glutamate = 4-(gamma-L-
CC glutamylamino)butanoy-[BtrI ACP] + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:53952, Rhea:RHEA-COMP:13744, Rhea:RHEA-COMP:13745,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137997, ChEBI:CHEBI:137998,
CC ChEBI:CHEBI:456216; EC=6.2.1.39;
CC Evidence={ECO:0000269|PubMed:15975512};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:15975512};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:15975512};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000305|PubMed:15975512};
CC -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC {ECO:0000269|PubMed:15975512}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15975512}.
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DR EMBL; AB097196; BAE07074.1; -; Genomic_DNA.
DR EMBL; AJ781030; CAG77428.2; -; Genomic_DNA.
DR AlphaFoldDB; Q4H4E7; -.
DR SMR; Q4H4E7; -.
DR KEGG; ag:BAE07074; -.
DR BioCyc; MetaCyc:MON-17271; -.
DR BRENDA; 6.2.1.39; 649.
DR UniPathway; UPA00964; -.
DR GO; GO:0016878; F:acid-thiol ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; ATP-binding; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding.
FT CHAIN 1..419
FT /note="[Butirosin acyl-carrier protein]--L-glutamate
FT ligase"
FT /id="PRO_0000421731"
FT DOMAIN 144..345
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 174..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 312
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 312
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 419 AA; 48648 MW; E474F046978F5BA4 CRC64;
MKFTHPLDYY RLNGKQILWY MNIGEDQDSQ ASNYFPSVKD PQSEKIVVQQ EQQLLFLARP
QDTVFFHTMP EQAFLDYWKE RRLSLPSIIC CDKLSQVPDL ERYTIIPFIV SDQLLELKRR
YPHMDIIAPD LAVCREINHK FNTRRLMERN GFNVTTGYFC SDIESLEHAY EQLISAGFSK
CVLKVPYGSS GKGLKVIDNE RNFRFLLNYI QNRQTNVDLL LEGWHPHRLS LTSQLFITEY
EVHLLAVTEQ IIDPNGVYKG TNFTPALSQS EAADYREEIL RAGELIRQMG YRGVLGIDSI
LDTNGELIPV IEINARLTQV TYILPLVIEQ KKRYEFVESR VLVFNSRADL DFEDYENDLS
EVTRDLPVRI DLYNFCKASG AFKNTYKLFV LVSAHNSEQL IKARSLLDEL NTKMTTAVH
