ID A0A0D3HQ35_9ORYZ Unreviewed; 429 AA.
AC A0A0D3HQ35;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART11G23230.2};
RN [1] {ECO:0000313|EnsemblPlants:OBART11G23230.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART11G23230.2};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART11G23230.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001688};
CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
CC {ECO:0000256|ARBA:ARBA00011412}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00009182}.
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DR AlphaFoldDB; A0A0D3HQ35; -.
DR STRING; 65489.A0A0D3HQ35; -.
DR PaxDb; 65489-OBART11G23230-2; -.
DR EnsemblPlants; OBART11G23230.2; OBART11G23230.2; OBART11G23230.
DR Gramene; OBART11G23230.2; OBART11G23230.2; OBART11G23230.
DR eggNOG; KOG1254; Eukaryota.
DR Proteomes; UP000026960; Chromosome 11.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.30.470.110; -; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [GDP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..204
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 242..423
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
SQ SEQUENCE 429 AA; 47431 MW; 1B344F99FD0863CD CRC64;
MARKKIREYD SKRLLKEHLK RLAGIDLQIL SAQVTQSTDF TELVNQQPWL STMKLVVKPD
MLFGKRGKSG LVALNLDIAQ VKEFVKERLG VEVEMGGCKA PITTFIVEPF VPHDQEYYLS
IVSERLGSTI SFSECGGIEI EENWDKVKTI FLSTEKPMTP DACAPLIATT LPLEARGKIG
DFIKGVFAVF QDLDFSFLEM NPFTIVNGEP YPLDMRGELD DTAAFKNFKK WGNIEFPLPF
GRVLSSTEGF IHDLDEKTSA SLKFTVLNPK GRIWTMVAGG GASVIYADTV SFEFLPYLGY
ASELENYAEY SGAPNEEEVL QYARVVLDCA TADPDGRKRA LLIGGGIANF TDIGATFSGI
IRALREKESK LKAARMHIYV RRGGPNYQTG LAKMRKLGAE LGVPIEVYGP EATMTGICKQ
AIECVMAAA
//