AACL2_BRADU
ID AACL2_BRADU Reviewed; 334 AA.
AC Q89GR3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Amino acid--[acyl-carrier-protein] ligase 2;
DE EC=6.2.1.n2;
DE AltName: Full=Amino acid:[carrier-protein] ligase [AMP forming] 2;
DE Short=aa:CP ligase 2;
DE AltName: Full=Aminoacyl-[acyl-carrier-protein] synthetase 2;
DE AltName: Full=L-glycine:[acyl-carrier-protein] ligase 2;
GN OrderedLocusNames=bll6282;
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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC
RP 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 blr6284 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=3.9 uM for carrier protein blr6284 {ECO:0000269|PubMed:20663952};
CC KM=0.58 mM for L-glycine {ECO:0000269|PubMed:20663952};
CC KM=14 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 -!- 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; BAC51547.1; -; Genomic_DNA.
DR RefSeq; NP_772922.1; NC_004463.1.
DR RefSeq; WP_011089022.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89GR3; -.
DR SMR; Q89GR3; -.
DR STRING; 224911.27354561; -.
DR EnsemblBacteria; BAC51547; BAC51547; BAC51547.
DR GeneID; 64026044; -.
DR KEGG; bja:bll6282; -.
DR PATRIC; fig|224911.44.peg.6260; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_054340_0_0_5; -.
DR InParanoid; Q89GR3; -.
DR OMA; NTHRNFF; -.
DR PhylomeDB; Q89GR3; -.
DR BRENDA; 6.2.1.B4; 929.
DR SABIO-RK; Q89GR3; -.
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 ATP-binding; Ligase; Metal-binding; Nucleotide-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..334
FT /note="Amino acid--[acyl-carrier-protein] ligase 2"
FT /id="PRO_0000401187"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 168..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /ligand_note="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 250..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 36803 MW; 1155D056C5D4C044 CRC64;
MNLAIVEAPA DSTPPPADPL DHLADALFHE MGSPGVYGRT ALYEDVVERI AAVISRNREP
NTEVMRFPPV MNRAQLERSG YLKSFPNLLG CVCGLHGIES EIDAAISRFD AGGDWTESLS
PADLVLSPAA CYPLYPIAAS RGPVPAAGWS FDVAADCFRR EPSRHLDRLQ SFRMREFVCI
GSADHVSAFR ERWIIRAQKI ARDLGLTFRI DHANDPFFGR VGQMMAVSQK QLSLKFELLV
PLRSEERPTA CMSFNYHRDH FGTTWGIVDA AGEPAHTACV AFGMDRLAVA MFHTHGKDVA
LWPIAVRDLL GLAQTDRGAP SAFEEYRCAK EAGS
