(data stored in SCRATCH zone)

SWISSPROT: C6WF99_ACTMD

ID   C6WF99_ACTMD            Unreviewed;       661 AA.
AC   C6WF99;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
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=Amir_0262 {ECO:0000313|EMBL:ACU34231.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34231.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34231.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(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}.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA. {ECO:0000256|HAMAP-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; CP001630; ACU34231.1; -; Genomic_DNA.
DR   RefSeq; WP_012782894.1; NC_013093.1.
DR   ProteinModelPortal; C6WF99; -.
DR   STRING; 446462.Amir_0262; -.
DR   EnsemblBacteria; ACU34231; ACU34231; Amir_0262.
DR   KEGG; ami:Amir_0262; -.
DR   eggNOG; ENOG4108IQF; Bacteria.
DR   eggNOG; COG0365; LUCA.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; DHWWHDL; -.
DR   OrthoDB; POG091H059D; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-HAMAP.
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   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   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; C6WF99.
DR   SWISS-2DPAGE; C6WF99.
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:ACU34231.1};
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:UP000002213}.
FT   DOMAIN       35     88       ACAS_N. {ECO:0000259|Pfam:PF16177}.
FT   DOMAIN       95    530       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      539    620       AMP-binding_C. {ECO:0000259|Pfam:
FT                                PF13193}.
FT   NP_BIND     393    395       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   NP_BIND     417    422       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   REGION      198    201       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       545    545       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       547    547       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       550    550       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     317    317       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     341    341       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     508    508       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     523    523       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     531    531       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     534    534       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   MOD_RES     620    620       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
SQ   SEQUENCE   661 AA;  71927 MW;  93A8E1C7C9F7CA8B CRC64;
     MTKPNENGPT LDNLLTESRT FPPSEEFAAQ ANATQALYDS AAADREAFWA EQADRLTWER
     KWDRVLDWSD APFAKWFVGG RLNVAYNCVD RHVESGHGEQ VAIHWEGEPG DSRTITYADL
     KRDVSKAANA LASLGVGAED RVAIYMPMVP EAIVAMLACA RIGALHSVVF GGFSAEALRT
     RVEDSQAKLV ITTDGQYRRG NPAPLKPAVD EAVSKAASVE HVLVVRRTGG EVAWTEGRDL
     WWHELVDGQS EEHAPEAFDS EHPLFILYTS GTTGNPKGIL HTSGGYLTQT AYTHHNVFDL
     KPDSDVYWCT ADIGWVTGHS YIVYGPLANR VTQVVYEGTP NTPHEGRHWE IVQKYGVSIY
     YTAPTLIRTF MKWGAEIPAK HDLSSLRVLG SVGEPINPEA WIWYRENIGA GKAPIVDTWW
     QTETGAIMIS PLPGVVSTKP GSAQRPLPGV GAKVVDDQGV EVGPGGGGYL VLDEPWPSML
     RGIWGDDARY RDTYWSRFAE EGFYFAGDGA KYDADGDIWL LGRVDDVMNV SGHRISTTEV
     ESALVSHPTV AEAAVVGATD PTTGQGIVAF VILRGGVAAG SDGAEAIKAL RDHVAKEIGP
     IAKPRQIMVV PELPKTRSGK IMRRLLRDVA ENRQVGDVTT LADSSVMDLI SSGLKKGSGE
     D
//

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