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

 AACL_AGRFC              Reviewed;         327 AA.
Q7CWR3;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
25-OCT-2017, entry version 62.
RecName: Full=Amino acid--[acyl-carrier-protein] ligase;
EC=6.2.1.n2;
AltName: Full=Amino acid:[carrier-protein] ligase [AMP forming];
Short=aa:CP ligase;
AltName: Full=Aminoacyl-[acyl-carrier-protein] synthetase;
AltName: Full=L-alanine:[acyl-carrier-protein] ligase;
AltName: Full=L-glycine:[acyl-carrier-protein] ligase;
AltName: Full=L-serine:[acyl-carrier-protein] ligase;
OrderedLocusNames=Atu2573; ORFNames=AGR_C_4663;
Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium
tumefaciens (strain C58)).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
Agrobacterium tumefaciens complex.
NCBI_TaxID=176299;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C58 / ATCC 33970;
PubMed=11743193; DOI=10.1126/science.1066804;
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
Nester E.W.;
"The genome of the natural genetic engineer Agrobacterium tumefaciens
C58.";
Science 294:2317-2323(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C58 / ATCC 33970;
PubMed=11743194; DOI=10.1126/science.1066803;
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
Cielo C., Slater S.;
"Genome sequence of the plant pathogen and biotechnology agent
Agrobacterium tumefaciens C58.";
Science 294:2323-2328(2001).
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC
PARAMETERS, AND SUBUNIT.
STRAIN=C58 / ATCC 33970;
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-alanine, and
to a lesser extent of L-glycine and L-serine, and their transfer
to the phosphopantetheine prosthetic group covalently attached to
the vicinal carrier protein Atu2571 of yet unknown function. May
participate in nonribosomal peptide synthesis or related
processes. L-proline and L-glutamate are very poor substrates
whereas 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=4.7 uM for carrier protein Atu2571
{ECO:0000269|PubMed:20663952};
KM=0.24 mM for L-alanine {ECO:0000269|PubMed:20663952};
KM=5.7 mM for L-glycine {ECO:0000269|PubMed:20663952};
KM=5.6 mM for L-serine {ECO:0000269|PubMed:20663952};
KM=46 mM for L-proline {ECO:0000269|PubMed:20663952};
KM=54 mM for L-glutamate {ECO:0000269|PubMed:20663952};
Note=The catalytic efficiency of the alanine activation reaction
is 27-fold and 44-fold higher than that of glycine and serine
activation, respectively.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20663952}.
-!- INTERACTION:
A9CHM9:Atu2571; NbExp=3; IntAct=EBI-16043272, EBI-16043291;
Q89VT6:bsr0959 (xeno); NbExp=2; IntAct=EBI-16043272, 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}.
-!- SEQUENCE CAUTION:
Sequence=AAK88296.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AE007869; AAK88296.2; ALT_INIT; Genomic_DNA.
RefSeq; NP_355511.2; NC_003062.2.
PDB; 4H2W; X-ray; 1.95 A; A/B=236-246.
PDB; 4H2X; X-ray; 2.15 A; A/B=236-246.
PDB; 4H2Y; X-ray; 2.10 A; A/B=236-246.
PDBsum; 4H2W; -.
PDBsum; 4H2X; -.
PDBsum; 4H2Y; -.
ProteinModelPortal; Q7CWR3; -.
SMR; Q7CWR3; -.
DIP; DIP-60153N; -.
IntAct; Q7CWR3; 2.
STRING; 176299.Atu2573; -.
EnsemblBacteria; AAK88296; AAK88296; Atu2573.
GeneID; 1134611; -.
KEGG; atu:Atu2573; -.
PATRIC; fig|176299.10.peg.2577; -.
eggNOG; COG0172; LUCA.
HOGENOM; HOG000177962; -.
BRENDA; 6.2.1.B5; 200.
SABIO-RK; Q7CWR3; -.
Proteomes; UP000000813; Chromosome circular.
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 1 327 Amino acid--[acyl-carrier-protein]
ligase.
/FTId=PRO_0000401188.
NP_BIND 183 184 ATP. {ECO:0000250}.
NP_BIND 265 268 ATP. {ECO:0000250}.
METAL 146 146 Zinc; catalytic. {ECO:0000250}.
METAL 191 191 Zinc; catalytic. {ECO:0000250}.
METAL 294 294 Zinc; catalytic. {ECO:0000250}.
BINDING 174 174 ATP. {ECO:0000250}.
BINDING 176 176 ATP. {ECO:0000250}.
BINDING 191 191 Amino acid substrate. {ECO:0000250}.
BINDING 250 250 ATP. {ECO:0000250}.
BINDING 301 301 ATP. {ECO:0000250}.
SEQUENCE 327 AA; 36344 MW; 06FEA577A833FD0E CRC64;
MTVFSAIPPI SCWFTGRTPA SWDKTMDMQT SFLDRLFEEG LLIETGVDGL YGRSGQFEDV
IAAFERLIDR TGGADGAEAI RFPPGINRAY FEKSGYMKSF PQLAGTVHSF CGCELDHVSL
LKSMDEGGDW TKDQKATDIV LTPAACYPLY PTIAKRGALP AGGGLYDIQS YCFRHEPSKD
PARQQLFRMR EYVCMGTESD VTEFRQTWMD RGVEMMKAVG LDVTIDIAND PFFGRAGKML
ANNQRDQNLK FELLIPVTSA TNPTACMSFN YHQDAFGQKW GLNLENGDVA HTACVGFGLE
RIALALFAHH GLDVKKWPAK VVETLWG


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