GENTAUR Molecular Products.

 AACL1_BRADU             Reviewed;         326 AA.
 Q89VT8;
 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
 01-JUN-2003, sequence version 1.
 28-FEB-2018, entry version 83.
 RecName: Full=Amino acid--[acyl-carrier-protein] ligase 1;
          EC=6.2.1.n2;
 AltName: Full=Amino acid:[carrier-protein] ligase [AMP forming] 1;
          Short=aa:CP ligase 1;
 AltName: Full=Aminoacyl-[acyl-carrier-protein] synthetase 1;
 AltName: Full=L-glycine:[acyl-carrier-protein] ligase 1;
 OrderedLocusNames=bll0957;
 Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC
 14792 / USDA 110).
 Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
 Bradyrhizobiaceae; Bradyrhizobium.
 NCBI_TaxID=224911;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110;
 PubMed=12597275; DOI=10.1093/dnares/9.6.189;
 Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
 Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
 Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
 Tabata S.;
 "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
 Bradyrhizobium japonicum USDA110.";
 DNA Res. 9:189-197(2002).
 [2]
 X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH ATP; ZINC AND
 SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
 COFACTOR, KINETIC PARAMETERS, AND SUBUNIT.
 STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110;
 PubMed=20663952; DOI=10.1073/pnas.1007470107;
 Mocibob M., Ivic N., Bilokapic S., Maier T., Luic M., Ban N.,
 Weygand-Durasevic I.;
 "Homologs of aminoacyl-tRNA synthetases acylate carrier proteins and
 provide a link between ribosomal and nonribosomal peptide synthesis.";
 Proc. Natl. Acad. Sci. U.S.A. 107:14585-14590(2010).
 -!- FUNCTION: Catalyzes the ATP-dependent activation of L-glycine and
     its transfer to the phosphopantetheine prosthetic group covalently
     attached to the vicinal carrier protein bsr0959 of yet unknown
     function. May participate in nonribosomal peptide synthesis or
     related processes. L-alanine is a poor substrate whereas L-serine
     or D-amino acids are not substrates for ATP-dependent activation.
     Does not display tRNA aminoacylation activity.
     {ECO:0000269|PubMed:20663952}.
 -!- CATALYTIC ACTIVITY: ATP + an amino acid + [acyl-carrier-protein] =
     AMP + diphosphate + an aminoacyl-[acyl-carrier-protein].
     {ECO:0000269|PubMed:20663952}.
 -!- COFACTOR:
     Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
       Evidence={ECO:0000269|PubMed:20663952};
     Note=Binds 1 Zn(2+) ion per subunit.
     {ECO:0000269|PubMed:20663952};
 -!- BIOPHYSICOCHEMICAL PROPERTIES:
     Kinetic parameters:
       KM=1.19 uM for carrier protein bsr0959
       {ECO:0000269|PubMed:20663952};
       KM=0.93 mM for L-glycine {ECO:0000269|PubMed:20663952};
       KM=25 mM for L-alanine {ECO:0000269|PubMed:20663952};
       Note=The catalytic efficiency of the glycine activation reaction
       is 300-fold higher than that of alanine activation.;
 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20663952}.
 -!- INTERACTION:
     Q89VT6:bsr0959; NbExp=4; IntAct=EBI-16043152, EBI-16043178;
 -!- MISCELLANEOUS: Lacks the N-terminal tRNA-binding domain compared
     to class-II aminoacyl-tRNA synthetases.
 -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
     family. Amino acid--[acyl-carrier-protein] ligase subfamily.
     {ECO:0000305}.
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 EMBL; BA000040; BAC46222.1; -; Genomic_DNA.
 RefSeq; NP_767597.1; NC_004463.1.
 RefSeq; WP_011083778.1; NZ_CP011360.1.
 PDB; 3MEY; X-ray; 2.50 A; A/B=1-326.
 PDB; 3MF1; X-ray; 2.20 A; A/B=1-326.
 PDB; 3MF2; X-ray; 2.15 A; A/B=1-326.
 PDB; 3PZC; X-ray; 2.20 A; A/B=1-326.
 PDB; 4H2S; X-ray; 2.15 A; A/B=1-326.
 PDB; 4H2T; X-ray; 2.44 A; A/B=1-326.
 PDB; 4H2U; X-ray; 2.10 A; A/B=1-326.
 PDB; 4H2V; X-ray; 2.00 A; A/B=1-326.
 PDB; 4H2W; X-ray; 1.95 A; A/B=1-220, A/B=232-326.
 PDB; 4H2X; X-ray; 2.15 A; A/B=1-220, A/B=232-326.
 PDB; 4H2Y; X-ray; 2.10 A; A/B=1-220, A/B=232-326.
 PDBsum; 3MEY; -.
 PDBsum; 3MF1; -.
 PDBsum; 3MF2; -.
 PDBsum; 3PZC; -.
 PDBsum; 4H2S; -.
 PDBsum; 4H2T; -.
 PDBsum; 4H2U; -.
 PDBsum; 4H2V; -.
 PDBsum; 4H2W; -.
 PDBsum; 4H2X; -.
 PDBsum; 4H2Y; -.
 ProteinModelPortal; Q89VT8; -.
 SMR; Q89VT8; -.
 DIP; DIP-60151N; -.
 IntAct; Q89VT8; 1.
 STRING; 224911.bll0957; -.
 EnsemblBacteria; BAC46222; BAC46222; BAC46222.
 GeneID; 1051747; -.
 KEGG; bja:bll0957; -.
 PATRIC; fig|224911.44.peg.345; -.
 eggNOG; ENOG41083GN; Bacteria.
 eggNOG; COG0172; LUCA.
 HOGENOM; HOG000177962; -.
 InParanoid; Q89VT8; -.
 OMA; VANDPFF; -.
 OrthoDB; POG091H0L1Z; -.
 PhylomeDB; Q89VT8; -.
 BioCyc; BDIA224911:G1G3J-966-MONOMER; -.
 BRENDA; 6.2.1.B4; 929.
 SABIO-RK; Q89VT8; -.
 EvolutionaryTrace; Q89VT8; -.
 Proteomes; UP000002526; Chromosome.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 1: Evidence at protein level;
 3D-structure; ATP-binding; Complete proteome; Ligase; Metal-binding;
 Nucleotide-binding; Reference proteome; Zinc.
 CHAIN         1    326       Amino acid--[acyl-carrier-protein] ligase
                              1.
                              /FTId=PRO_0000401186.
 NP_BIND     168    169       ATP.
 NP_BIND     250    253       ATP.
 METAL       131    131       Zinc; catalytic.
 METAL       176    176       Zinc; catalytic.
 METAL       279    279       Zinc; catalytic.
 BINDING     159    159       ATP.
 BINDING     161    161       ATP.
 BINDING     176    176       Amino acid substrate.
 BINDING     235    235       ATP.
 BINDING     286    286       ATP.
 STRAND       12     19       {ECO:0000244|PDB:4H2W}.
 HELIX        20     31       {ECO:0000244|PDB:4H2W}.
 STRAND       36     39       {ECO:0000244|PDB:4H2W}.
 HELIX        41     56       {ECO:0000244|PDB:4H2W}.
 STRAND       62     66       {ECO:0000244|PDB:4H2W}.
 STRAND       69     72       {ECO:0000244|PDB:4H2W}.
 HELIX        73     79       {ECO:0000244|PDB:4H2W}.
 HELIX        81     83       {ECO:0000244|PDB:4H2W}.
 HELIX        86     88       {ECO:0000244|PDB:4H2W}.
 STRAND       91     94       {ECO:0000244|PDB:4H2W}.
 HELIX        99    110       {ECO:0000244|PDB:4H2W}.
 HELIX       115    118       {ECO:0000244|PDB:4H2W}.
 STRAND      120    126       {ECO:0000244|PDB:4H2W}.
 STRAND      128    131       {ECO:0000244|PDB:4H2W}.
 HELIX       134    139       {ECO:0000244|PDB:4H2W}.
 STRAND      149    158       {ECO:0000244|PDB:4H2W}.
 STRAND      170    181       {ECO:0000244|PDB:4H2W}.
 HELIX       183    203       {ECO:0000244|PDB:4H2W}.
 STRAND      209    212       {ECO:0000244|PDB:4H2W}.
 HELIX       219    231       {ECO:0000244|PDB:4H2W}.
 STRAND      235    240       {ECO:0000244|PDB:4H2W}.
 STRAND      245    247       {ECO:0000244|PDB:4H2W}.
 STRAND      249    256       {ECO:0000244|PDB:4H2W}.
 HELIX       260    265       {ECO:0000244|PDB:4H2W}.
 STRAND      272    274       {ECO:0000244|PDB:4H2V}.
 STRAND      276    283       {ECO:0000244|PDB:4H2V}.
 HELIX       285    287       {ECO:0000244|PDB:4H2W}.
 HELIX       288    291       {ECO:0000244|PDB:4H2W}.
 STRAND      292    297       {ECO:0000244|PDB:4H2W}.
 HELIX       299    301       {ECO:0000244|PDB:4H2W}.
 HELIX       304    310       {ECO:0000244|PDB:4H2W}.
 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

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