AACL_AGRFC
ID AACL_AGRFC Reviewed; 327 AA.
AC Q7CWR3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Amino acid--[acyl-carrier-protein] ligase;
DE EC=6.2.1.n2;
DE AltName: Full=Amino acid:[carrier-protein] ligase [AMP forming];
DE Short=aa:CP ligase;
DE AltName: Full=Aminoacyl-[acyl-carrier-protein] synthetase;
DE AltName: Full=L-alanine:[acyl-carrier-protein] ligase;
DE AltName: Full=L-glycine:[acyl-carrier-protein] ligase;
DE AltName: Full=L-serine:[acyl-carrier-protein] ligase;
GN OrderedLocusNames=Atu2573; ORFNames=AGR_C_4663;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC
RP PARAMETERS, AND SUBUNIT.
RC STRAIN=C58 / ATCC 33970;
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-alanine, and to a
CC lesser extent of L-glycine and L-serine, and their transfer to the
CC phosphopantetheine prosthetic group covalently attached to the vicinal
CC carrier protein Atu2571 of yet unknown function. May participate in
CC nonribosomal peptide synthesis or related processes. L-proline and L-
CC glutamate are very poor substrates whereas 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=4.7 uM for carrier protein Atu2571 {ECO:0000269|PubMed:20663952};
CC KM=0.24 mM for L-alanine {ECO:0000269|PubMed:20663952};
CC KM=5.7 mM for L-glycine {ECO:0000269|PubMed:20663952};
CC KM=5.6 mM for L-serine {ECO:0000269|PubMed:20663952};
CC KM=46 mM for L-proline {ECO:0000269|PubMed:20663952};
CC KM=54 mM for L-glutamate {ECO:0000269|PubMed:20663952};
CC Note=The catalytic efficiency of the alanine activation reaction is
CC 27-fold and 44-fold higher than that of glycine and serine
CC activation, respectively.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20663952}.
CC -!- INTERACTION:
CC Q7CWR3; A9CHM9: Atu2571; NbExp=3; IntAct=EBI-16043272, EBI-16043291;
CC Q7CWR3; Q89VT6: bsr0959; Xeno; NbExp=2; IntAct=EBI-16043272, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK88296.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007869; AAK88296.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_355511.2; NC_003062.2.
DR PDB; 4H2W; X-ray; 1.95 A; A/B=236-246.
DR PDB; 4H2X; X-ray; 2.15 A; A/B=236-246.
DR PDB; 4H2Y; X-ray; 2.10 A; A/B=236-246.
DR PDBsum; 4H2W; -.
DR PDBsum; 4H2X; -.
DR PDBsum; 4H2Y; -.
DR AlphaFoldDB; Q7CWR3; -.
DR SMR; Q7CWR3; -.
DR DIP; DIP-60153N; -.
DR IntAct; Q7CWR3; 2.
DR STRING; 176299.Atu2573; -.
DR EnsemblBacteria; AAK88296; AAK88296; Atu2573.
DR KEGG; atu:Atu2573; -.
DR PATRIC; fig|176299.10.peg.2577; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_054340_0_0_5; -.
DR BRENDA; 6.2.1.B5; 200.
DR SABIO-RK; Q7CWR3; -.
DR Proteomes; UP000000813; Chromosome circular.
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..327
FT /note="Amino acid--[acyl-carrier-protein] ligase"
FT /id="PRO_0000401188"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 183..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /ligand_note="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 265..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ 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
