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Amino acid--[acyl-carrier-protein] ligase 1 (EC 6.2.1.n2) (Amino acid:[carrier-protein] ligase [AMP forming] 1) (aa:CP ligase 1) (Aminoacyl-[acyl-carrier-protein] synthetase 1) (L-glycine:[acyl-carrier-protein] ligase 1)

 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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