ID   Q57XD7_TRYB2            Unreviewed;       673 AA.
AC   Q57XD7; D6XKY9;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   Name=Tb08.26A17.430 {ECO:0000313|EMBL:AAZ13019.1};
GN   ORFNames=Tb927.8.2520 {ECO:0000313|EMBL:AAX69719.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|EMBL:AAX69719.1, ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:AAZ13019.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ13019.1};
RX   PubMed=16020724; DOI=10.1126/science.1112181;
RA   El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA   Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA   Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA   Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA   Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA   Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA   Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA   Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA   Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT   "Comparative genomics of trypanosomatid parasitic protozoa.";
RL   Science 309:404-409(2005).
RN   [2] {ECO:0000313|EMBL:AAZ13019.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ13019.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [3] {ECO:0000313|EMBL:AAX69719.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX69719.1};
RA   Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA   Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA   Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA   Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA   Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT   ".";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AAZ13019.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ13019.1};
RA   Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA   Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA   Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA   Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA   Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT   "Sequencing, closure, and annotation of Trypanosoma brucei chromosomes 2
RT   through 8.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|RuleBase:RU361147};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|RuleBase:RU361147}.
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; AC159420; AAX69719.1; -; Genomic_DNA.
DR   EMBL; CP000071; AAZ13019.1; -; Genomic_DNA.
DR   RefSeq; XP_847085.1; XM_841992.1.
DR   AlphaFoldDB; Q57XD7; -.
DR   STRING; 185431.Q57XD7; -.
DR   SwissPalm; Q57XD7; -.
DR   PaxDb; 5691-AAZ13019; -.
DR   GeneID; 3659232; -.
DR   KEGG; tbr:Tb927.8.2520; -.
DR   VEuPathDB; TriTrypDB:Tb927.8.2520; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   InParanoid; Q57XD7; -.
DR   OMA; AIKASWP; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000008524; Chromosome 8.
DR   GO; GO:0097014; C:ciliary plasm; IDA:GeneDB.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
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-UniRule.
DR   GO; GO:0003824; F:catalytic activity; ISM:GeneDB.
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   CDD; cd05966; ACS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361147};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361147};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524}.
FT   DOMAIN          35..96
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          98..492
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          553..632
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  74666 MW;  4E2CFD509EB14D8E CRC64;
     MRDTGRCSGH NDDVVDPVTS NGAMSHVGPD LAHRQALYEE SVRDPVAFWE QAAADFHWER
     TWPKDKSPLE YNFHKSNGSI FVKWFDGAES NMCYNALDRH LPKHKDRVCY HWEGNDEGES
     RDVTYGEMFE EVVRIAAVLK HRYNVKKGDV VTIYLPMIPF AAQVMLAVAR LGAVTSVVFA
     GFSSQAVASR LTDARSKLII TADSFWRGTK TLLLKELSDA ALAICEAEGH NVQCLVYDRS
     KRENVPMTEG RDAWYSDVVE TLTASELADC PIVWIGAEDP LFLLYTSGST GKPKAILHTL
     GGYMVYAGVT FKYSFDYHES DVSFCTADIG WITGHSYALY GPMLNAATSV LFEGMPTHPT
     PSRWWDLVDK YRVTIFYTAP TAIRALMQCG DEHLQSTTRG TLRILGSVGE PINAEAWQWF
     YEVVGKRRAD VIDTWWQTET GGHLITPLPG CTPMKAGSAT LPFFGIVPAL LHPTTNAVVE
     GEGEGLLAMQ TPWPGIARTI FGDHNRYEQA YFAVDGFYLT GDGARRDKDG YYWITGRVDD
     VLNVSGHRIG TSEVEEAVNS HPDVAESAAV GIPHDVKGEC IYVFVTFNNN VTVDATLLKR
     VRETVRRVIG PFAAPDYVQA AQCGLPKTRS GKIMRRILRK IASGLHEELG DTSTLLDPSV
     VQNLIEGRKQ TVG
//