AACL1_BRADU
ID AACL1_BRADU Reviewed; 326 AA.
AC Q89VT8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Amino acid--[acyl-carrier-protein] ligase 1;
DE EC=6.2.1.n2;
DE AltName: Full=Amino acid:[carrier-protein] ligase [AMP forming] 1;
DE Short=aa:CP ligase 1;
DE AltName: Full=Aminoacyl-[acyl-carrier-protein] synthetase 1;
DE AltName: Full=L-glycine:[acyl-carrier-protein] ligase 1;
GN OrderedLocusNames=bll0957;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH ATP; ZINC AND
RP SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP COFACTOR, KINETIC PARAMETERS, AND SUBUNIT.
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=20663952; DOI=10.1073/pnas.1007470107;
RA Mocibob M., Ivic N., Bilokapic S., Maier T., Luic M., Ban N.,
RA Weygand-Durasevic I.;
RT "Homologs of aminoacyl-tRNA synthetases acylate carrier proteins and
RT provide a link between ribosomal and nonribosomal peptide synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14585-14590(2010).
CC -!- FUNCTION: Catalyzes the ATP-dependent activation of L-glycine and its
CC transfer to the phosphopantetheine prosthetic group covalently attached
CC to the vicinal carrier protein bsr0959 of yet unknown function. May
CC participate in nonribosomal peptide synthesis or related processes. L-
CC alanine is a poor substrate whereas L-serine or D-amino acids are not
CC substrates for ATP-dependent activation. Does not display tRNA
CC aminoacylation activity. {ECO:0000269|PubMed:20663952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + ATP + holo-[ACP] = AMP + an L-alpha-
CC aminoacyl-[ACP] + diphosphate; Xref=Rhea:RHEA:52660, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:13877, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59869, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138175, ChEBI:CHEBI:456215; EC=6.2.1.n2;
CC Evidence={ECO:0000269|PubMed:20663952};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20663952};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:20663952};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.19 uM for carrier protein bsr0959 {ECO:0000269|PubMed:20663952};
CC KM=0.93 mM for L-glycine {ECO:0000269|PubMed:20663952};
CC KM=25 mM for L-alanine {ECO:0000269|PubMed:20663952};
CC Note=The catalytic efficiency of the glycine activation reaction is
CC 300-fold higher than that of alanine activation.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20663952}.
CC -!- INTERACTION:
CC Q89VT8; Q89VT6: bsr0959; NbExp=4; IntAct=EBI-16043152, EBI-16043178;
CC -!- MISCELLANEOUS: Lacks the N-terminal tRNA-binding domain compared to
CC class-II aminoacyl-tRNA synthetases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Amino acid--[acyl-carrier-protein] ligase subfamily. {ECO:0000305}.
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DR EMBL; BA000040; BAC46222.1; -; Genomic_DNA.
DR RefSeq; NP_767597.1; NC_004463.1.
DR RefSeq; WP_011083778.1; NZ_CP011360.1.
DR PDB; 3MEY; X-ray; 2.50 A; A/B=1-326.
DR PDB; 3MF1; X-ray; 2.20 A; A/B=1-326.
DR PDB; 3MF2; X-ray; 2.15 A; A/B=1-326.
DR PDB; 3PZC; X-ray; 2.20 A; A/B=1-326.
DR PDB; 4H2S; X-ray; 2.15 A; A/B=1-326.
DR PDB; 4H2T; X-ray; 2.44 A; A/B=1-326.
DR PDB; 4H2U; X-ray; 2.10 A; A/B=1-326.
DR PDB; 4H2V; X-ray; 2.00 A; A/B=1-326.
DR PDB; 4H2W; X-ray; 1.95 A; A/B=1-220, A/B=232-326.
DR PDB; 4H2X; X-ray; 2.15 A; A/B=1-220, A/B=232-326.
DR PDB; 4H2Y; X-ray; 2.10 A; A/B=1-220, A/B=232-326.
DR PDBsum; 3MEY; -.
DR PDBsum; 3MF1; -.
DR PDBsum; 3MF2; -.
DR PDBsum; 3PZC; -.
DR PDBsum; 4H2S; -.
DR PDBsum; 4H2T; -.
DR PDBsum; 4H2U; -.
DR PDBsum; 4H2V; -.
DR PDBsum; 4H2W; -.
DR PDBsum; 4H2X; -.
DR PDBsum; 4H2Y; -.
DR AlphaFoldDB; Q89VT8; -.
DR SMR; Q89VT8; -.
DR DIP; DIP-60151N; -.
DR IntAct; Q89VT8; 1.
DR STRING; 224911.27349207; -.
DR EnsemblBacteria; BAC46222; BAC46222; BAC46222.
DR GeneID; 64020820; -.
DR KEGG; bja:bll0957; -.
DR PATRIC; fig|224911.44.peg.345; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_054340_0_0_5; -.
DR InParanoid; Q89VT8; -.
DR OMA; RFPPVMS; -.
DR PhylomeDB; Q89VT8; -.
DR BRENDA; 6.2.1.B4; 929.
DR SABIO-RK; Q89VT8; -.
DR EvolutionaryTrace; Q89VT8; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR SUPFAM; SSF55681; SSF55681; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..326
FT /note="Amino acid--[acyl-carrier-protein] ligase 1"
FT /id="PRO_0000401186"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 168..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 176
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /ligand_note="substrate"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 250..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 41..56
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 170..181
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 183..203
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4H2W"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4H2W"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:4H2W"
SQ SEQUENCE 326 AA; 35942 MW; 22DB7DAAD6AF36EF CRC64;
MNIAVLPNSP DTAPQIADPL DHLADKLFHS MGSDGVYART ALYESIVERL AALITSHREA
GTEALRFPPV MSRAQLEKSG YLKSFPNLLG CVCGLHGTER EINAAVSRFD AGGDWTTSLS
PADLVLSPAA CYPVYPIAAS RGPLPKGGLR FDVAADCFRR EPSKHLDRLQ SFRMREYVCI
GTPDDVSDFR ERWMVRAQAI ARDLGLTFRV DYASDPFFGR VGQMKAVSQK QQQLKFELLI
PLRSEEQPTA CMSFNYHREH FGTTWGIQDA NGEPAHTGCV AFGMDRLAVA MFHTHGTDLS
AWPAKVRDIL GLQPHVAAGA HGEGWR
