(data stored in SCRATCH zone)

SWISSPROT: E6S985_INTC7

ID   E6S985_INTC7            Unreviewed;       658 AA.
AC   E6S985;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 42.
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=Intca_0516 {ECO:0000313|EMBL:ADU47061.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU47061.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU47061.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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}.
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};
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; CP002343; ADU47061.1; -; Genomic_DNA.
DR   RefSeq; WP_013491382.1; NC_014830.1.
DR   STRING; 710696.Intca_0516; -.
DR   EnsemblBacteria; ADU47061; ADU47061; Intca_0516.
DR   KEGG; ica:Intca_0516; -.
DR   eggNOG; ENOG4108IQF; Bacteria.
DR   eggNOG; COG0365; LUCA.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OrthoDB; 141801at2; -.
DR   Proteomes; UP000008914; 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; E6S985.
DR   SWISS-2DPAGE; E6S985.
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:ADU47061.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914}.
FT   DOMAIN       29     82       ACAS_N. {ECO:0000259|Pfam:PF16177}.
FT   DOMAIN       89    524       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      533    618       AMP-binding_C. {ECO:0000259|Pfam:
FT                                PF13193}.
FT   NP_BIND     389    391       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   NP_BIND     413    418       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       541    541       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     313    313       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   BINDING     528    528       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   MOD_RES     618    618       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
SQ   SEQUENCE   658 AA;  71897 MW;  678660EA24A7E85D CRC64;
     MSETLENLLQ ETRTFPPPPE FASRANGTAE LYEKADADHE GFWAEQARTY VSWSKDFTQT
     LQWDTPFAKW FPDGELNACY NAVDRHVEAG NGDRVAIHWI GEPEGDTREI TYSDLHSSVQ
     RAANALQDIG VRKGDTVAIY LPMIPEAAVA MLACARIGAP HSVVFGGFSA EALHSRIDDA
     GAKVVITSDG GYRRGSASPL KPAVDAALDH GDTSVEKVLV VKRTGQETPW TEGRDLWWDE
     VLEQAAPTHE APAHESEHPL FILYTSGTTG KPKGIFHTTG GYLTQCAYTN AVVHDVHPES
     DVYWCTADIG WVTGHSYIVY GPLTLGATQV MYEGTPDTPH QGRFWEIVEQ KKVTILYTAP
     TAIRTFMKWG DDIPGKFDLS SLRLLGSVGE PINPEAWMWY RRVIGGDRCP IVDTWWQTET
     GAIMVSPLPG VTATKPGSAQ RAIPGIGAEV VDDMAQPVPN GHGGYLVLTK PWPAMLRGIW
     GDPERYKETY WSRFEGLYFA GDGAKKDDDG DIWLLGRVDD VMNVSGHRLS TTEIESALVS
     HPKVAEAAVV GATDETTGQA VVAFVILRSE AVAEADEPGE GADIVAELRN HVAKEIGPIA
     KPRSIMIVPE LPKTRSGKIM RRLLRDVAEN RQVGDVTTLA DSSVMELIKT GLNKGDGD
//

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