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ACSA_BRADU
ID   ACSA_BRADU              Reviewed;         648 AA.
AC   Q89WV5; Q93Q03;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
GN   Name=acsA {ECO:0000255|HAMAP-Rule:MF_01123}; OrderedLocusNames=blr0573;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-605, AND MUTAGENESIS OF GLY-263;
RP   GLY-266; LYS-269 AND GLU-414.
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=11726281; DOI=10.1093/oxfordjournals.jbchem.a003052;
RA   Lee H.Y., Na K.B., Koo H.M., Kim Y.S.;
RT   "Identification of active site residues in Bradyrhizobium japonicum acetyl-
RT   CoA synthetase.";
RL   J. Biochem. 130:807-813(2001).
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC       an essential intermediate at the junction of anabolic and catabolic
CC       pathways. AcsA undergoes a two-step reaction. In the first half
CC       reaction, AcsA combines acetate with ATP to form acetyl-adenylate
CC       (AcAMP) intermediate. In the second half reaction, it can then transfer
CC       the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC       product AcCoA. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01123};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK95494.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BA000040; BAC45838.1; -; Genomic_DNA.
DR   EMBL; AF290478; AAK95494.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; NP_767213.1; NC_004463.1.
DR   RefSeq; WP_028174953.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89WV5; -.
DR   SMR; Q89WV5; -.
DR   STRING; 224911.27348822; -.
DR   EnsemblBacteria; BAC45838; BAC45838; BAC45838.
DR   GeneID; 64020436; -.
DR   KEGG; bja:blr0573; -.
DR   PATRIC; fig|224911.44.peg.9115; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_3_6_5; -.
DR   InParanoid; Q89WV5; -.
DR   OMA; DHWWHDL; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   HAMAP; MF_01123; Ac_CoA_synth; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..648
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208355"
FT   BINDING         190..193
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         308
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         332
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         384..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         408..413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         512
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         520
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         534
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         536
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         581
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   MOD_RES         606
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   MUTAGEN         263
FT                   /note="G->I: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11726281"
FT   MUTAGEN         266
FT                   /note="G->I: Great decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11726281"
FT   MUTAGEN         269
FT                   /note="K->G: Great decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11726281"
FT   MUTAGEN         414
FT                   /note="E->Q: Great decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11726281"
SQ   SEQUENCE   648 AA;  72030 MW;  4D439C3AF01483B0 CRC64;
     MSEKIYDVPA EWAKRAWVDQ AKYKEMYARS ISDPNGFWAE QAKRIDWMKA PTKIENVSFA
     PGNVSIKWFE DGVLNVAHNC IDRHLHKRAN QTAIIWEGDD PSQSRHITYK ELHDEVCRMA
     NILRTRNVKK GDRVTIYLPM IPEAAYAMLA CARIGAIHSV VFAGFSPDSL AQRINDCQSK
     VIITADEGLR GGKKVPLKAN VDAALAKADG VDWVVVVKRT GGKIDMNPTR DLWYHEAAAM
     VTTECPVEHM HAEDPLFILY TSGSTGQPKG VLHTSAGYLV YAAMTHQYVF DYHDGDIYWC
     TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPDNSRFW NVIDKHKVNT FYTAPTAIRA
     LMQGGDEPVK KTSRASLRLL GSVGEPINPE AWEWYHRVVG EDRCPIVDTW WQTETGGILI
     TPLPGATKLK PGSATQPFFG VVPEIVDADG KVLEGETTGN LCLTRAWPGM MRTVYGDHAR
     FEQTYFSTYK GKYFTGDGCR RDADGYYWIT GRVDDVINVS GHRMGTAEVE SALVAHEKVS
     EAAVVGFPHD IKGQGIYAYV TLMAGVQPTE DLRKELVTWV RKEIGPIASP DQIQFAPGLP
     KTRSGKIMRR ILRKIAEDEP GSLGDTSTLA DPAVVDDLVK NRQNKKSA
 
 
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