ID Q6H798_ORYSJ Unreviewed; 705 AA.
AC Q6H798; Q0E0S9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN OrderedLocusNames=Os02g0525900 {ECO:0000313|EMBL:BAS78985.1};
GN ORFNames=OSNPB_020525900 {ECO:0000313|EMBL:BAS78985.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000313|EMBL:BAS78985.1, ECO:0000313|Proteomes:UP000059680};
RN [1] {ECO:0000313|EMBL:BAG89807.1}
RP NUCLEOTIDE SEQUENCE.
RA Kikuchi S., Satoh K., Nagata T., Kawagashira N., Doi K., Kishimoto N.,
RA Yazaki J., Ishikawa M., Yamada H., Ooka H., Hotta I., Kojima K., Namiki T.,
RA Ohneda E., Yahagi W., Suzuki K., Li C., Ohtsuki K., Shishiki T., Otomo Y.,
RA Murakami K., Iida Y., Sugano S., Fujimura T., Suzuki Y., Tsunoda Y.,
RA Kurosaki T., Kodama T., Masuda H., Kobayashi M., Xie Q., Lu M.,
RA Narikawa R., Sugiyama A., Mizuno K., Yokomizo S., Niikura J., Ikeda R.,
RA Ishibiki J., Kawamata M., Yoshimura A., Miura J., Kusumegi T., Oka M.,
RA Ryu R., Ueda M., Matsubara K., Kawai J., Carninci P., Adachi J., Aizawa K.,
RA Arakawa T., Fukuda S., Hara A., Hashidume W., Hayatsu N., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Kondo S., Konno H., Miyazaki A., Osato N.,
RA Ota Y., Saito R., Sasaki D., Sato K., Shibata K., Shinagawa A., Shiraki T.,
RA Yoshino M., Hayashizaki Y.;
RT "Collection, Mapping, and Annotation of Over 28,000 cDNA Clones from
RT japonica Rice.";
RL Science 301:376-379(2003).
RN [2] {ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3] {ECO:0000313|EMBL:BAS78985.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23299411; DOI=10.1093/pcp/pcs183;
RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., Wakimoto H.,
RA Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., Inokuchi H., Ikemura T.,
RA Matsumoto T., Sasaki T., Itoh T.;
RT "Rice Annotation Project Database (RAP-DB): an integrative and interactive
RT database for rice genomics.";
RL Plant Cell Physiol. 54:E6-E6(2013).
RN [4] {ECO:0000313|EMBL:BAS78985.1, ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5] {ECO:0000313|EMBL:BAS78985.1}
RP NUCLEOTIDE SEQUENCE.
RA Sakai H., Kawahara Y., Matsumoto T., Buell C.R., Itoh T.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00034252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642;
CC Evidence={ECO:0000256|ARBA:ARBA00034252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumarate + ATP + H(+) = (E)-4-coumaroyl-AMP +
CC diphosphate; Xref=Rhea:RHEA:72419, ChEBI:CHEBI:12876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:192348; Evidence={ECO:0000256|ARBA:ARBA00034219};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72420;
CC Evidence={ECO:0000256|ARBA:ARBA00034219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H(+);
CC Xref=Rhea:RHEA:72423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:85008, ChEBI:CHEBI:192348, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72424;
CC Evidence={ECO:0000256|ARBA:ARBA00034223};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU361147}.
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DR EMBL; AK066073; BAG89807.1; -; mRNA.
DR EMBL; AP014958; BAS78985.1; -; Genomic_DNA.
DR RefSeq; XP_015626476.1; XM_015770990.1.
DR AlphaFoldDB; Q6H798; -.
DR SMR; Q6H798; -.
DR STRING; 39947.Q6H798; -.
DR PaxDb; 39947-Q6H798; -.
DR EnsemblPlants; Os02t0525900-01; Os02t0525900-01; Os02g0525900.
DR EnsemblPlants; Os02t0525900-02; Os02t0525900-02; Os02g0525900.
DR GeneID; 4329518; -.
DR Gramene; Os02t0525900-01; Os02t0525900-01; Os02g0525900.
DR Gramene; Os02t0525900-02; Os02t0525900-02; Os02g0525900.
DR KEGG; osa:4329518; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR OMA; INVSYNC; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6H798; baseline and differential.
DR GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
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:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
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 GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|ProteomicsDB:Q6H798};
KW Reference proteome {ECO:0000313|Proteomes:UP000059680}.
FT DOMAIN 71..132
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 139..527
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 589..667
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 705 AA; 77592 MW; 8C11E521B57F67BE CRC64;
MGTASGDQPA GASSDKLRHV ESMSELPSGA GRISGINAVV LGESLAAEEH DLVYPSAEFS
ADALVPSPKK YQKMYERSIN DPAGFWSEIA DAFYWKEKWN PSEVCSENLD VTKGPVQISW
FKGGKTNICY NAVDRNVEAG NGDKIAMYWE GNEPGQDGKL TYSELLDRVC QLANYLKSVG
VGKGDAVIIY LPMLLELPIA MLACARIGAV HSVVFAGFSA DSLAQRIVDC KPKLVITCNA
VKRGVKPILL KDIVDAGLAE SEKQGVAVGL CLTYENQSAM KREDTKWQAG RDVWWQDVVT
SFPTKCDVEW VDAEDPLFLL YTSGSTGKPK GVLHTTGGYM VYSATTFKYA FDYKPSDIYW
CTADCGWITG HSYVTYGPLL NGATVLVFEG TPNYPDSGRC WDIVDKYKVT IFYTAPTLVR
SLMRDGTEYV TRHSRKSLRV LGSVGEPINP SAWRWFYNIV GDSRCPISDT WWQTETGGFM
ITPLPGAWPQ KPGSATFPFF GVQPVIVDEK GKEIEGECSG YLCIKKSWPG AFRTLYGDHD
RYETTYFKPF AGYYFTGDGC SRDKDGYHWL TGRVDDVINV SGHRIGTAEV ESALVSHPKC
AEAAVVAVEH EVKGQGIYAF VTLVDGVPYS EELRKSLILT VRNQIGAFAA PDKIHWAPGL
PKTRSGKIMR RILRKIASKQ LDELGDTSTL ADPGVVDQLI ALKDC
//
