(data stored in ACNUC7421 zone)

SWISSPROT: C7QH83_CATAD

ID   C7QH83_CATAD            Unreviewed;       651 AA.
AC   C7QH83;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123};
GN   Name=acsA {ECO:0000256|HAMAP-Rule:MF_01123};
GN   OrderedLocusNames=Caci_0067 {ECO:0000313|EMBL:ACU69022.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69022.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69022.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC       (AcCoA), an essential intermediate at the junction of anabolic and
CC       catabolic pathways. AcsA undergoes a two-step reaction. In the
CC       first half reaction, AcsA combines acetate with ATP to form
CC       acetyl-adenylate (AcAMP) intermediate. In the second half
CC       reaction, it can then transfer the acetyl group from AcAMP to the
CC       sulfhydryl group of CoA, forming the product AcCoA.
CC       {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000256|SAAS:SAAS00711888}.
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:0000256|HAMAP-
CC         Rule:MF_01123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01123, ECO:0000256|SAAS:SAAS00711884};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
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DR   EMBL; CP001700; ACU69022.1; -; Genomic_DNA.
DR   RefSeq; WP_012784317.1; NC_013131.1.
DR   STRING; 479433.Caci_0067; -.
DR   EnsemblBacteria; ACU69022; ACU69022; Caci_0067.
DR   KEGG; cai:Caci_0067; -.
DR   eggNOG; ENOG4108IQF; Bacteria.
DR   eggNOG; COG0365; LUCA.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; WFYNIVG; -.
DR   OrthoDB; 141801at2; -.
DR   BioCyc; CACI479433:G1GFP-69-MONOMER; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
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:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   CDD; cd05966; ACS; 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; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; AMP-dep_Synthh-like_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   3: Inferred from homology;
DR   PRODOM; C7QH83.
DR   SWISS-2DPAGE; C7QH83.
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:ACU69022.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01123,
KW   ECO:0000256|SAAS:SAAS00711869};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123,
KW   ECO:0000256|SAAS:SAAS00711886};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN       31     83       ACAS_N. {ECO:0000259|Pfam:PF16177}.
FT   DOMAIN       90    524       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      533    611       AMP-binding_C. {ECO:0000259|Pfam:
FT                                PF13193}.
FT   NP_BIND     387    389       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   NP_BIND     411    416       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   REGION      193    196       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       539    539       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       544    544       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     311    311       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     502    502       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     517    517       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     525    525       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   MOD_RES     611    611       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
SQ   SEQUENCE   651 AA;  70768 MW;  F815FC418DF7CC8E CRC64;
     MSNEALSNLL REDRRFAPSA AFAADANVKA DAYAAAEADR LAFWDTQASR LSWDTPWSET
     LDWSGMPVAK WFVGGKLNVA YNCVDRHVEA GNGDRVAIHF EGEPGDSRAI TYAELKDEVS
     KAANALTELG VRQGDRVAIY MPMIPETAVA MLACARIGAV HSVVFAAFSP DALRARIEDA
     GAKLLITADG YHRRGGTVNL KANADEAVNG AETIENVLVV KRTGADVAWG DKDVWWHDAV
     GGASTEHTPE AFDSENPLFI LYTSGTTGKP KGILHTTGGY LTQASYTHHA VFDLKPESDV
     YWCTADVGWV TGHSYIVYGP LSNGVTEVMY EGTPDTPHQG RFWEIIQKYK VSLLYTAPTA
     IRMFAKWGDD IPAKFDLSSL RLLGSVGEPI NPEAWIWYRK NIGGDRTPVV DTWWQTETGA
     IMISPLPGVT EAKPGSAMRP LPGISANVVD KDGNIVGNGH GGLLVLDKPW PSMARGIWGD
     QQRFIDTYWA RFAEQGYYFA GDGAKKDEDG DLWLLGRVDD IMLVSGHNIS TTEVESALVS
     YPAVAEAAVV GAKDETTGQR IVAFVILRAG QEETEGLDAA LKAHVSKEIG PIAKPKQIQI
     VPELPKTRSG KIMRRLLKDV AEDRVVGDTT TLADSTVMDL IKAKLPHANE D
//

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