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Database: UniProt
Entry: A0A109FAT6_9BASI
LinkDB: A0A109FAT6_9BASI
Original site: A0A109FAT6_9BASI 
ID   A0A109FAT6_9BASI        Unreviewed;      1135 AA.
AC   A0A109FAT6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=ATP-citrate synthase {ECO:0000256|PIRNR:PIRNR036511};
DE            EC=2.3.3.8 {ECO:0000256|PIRNR:PIRNR036511};
DE   AltName: Full=ATP-citrate (pro-S-)-lyase {ECO:0000256|PIRNR:PIRNR036511};
DE   AltName: Full=Citrate cleavage enzyme {ECO:0000256|PIRNR:PIRNR036511};
GN   ORFNames=RHOSPDRAFT_30672 {ECO:0000313|EMBL:KWU41037.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU41037.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU41037.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU41037.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|PIRNR:PIRNR036511};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|PIRNR:PIRNR036511}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC       CoA ligase alpha subunit family. {ECO:0000256|ARBA:ARBA00005899,
CC       ECO:0000256|PIRNR:PIRNR036511}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC       CoA ligase beta subunit family. {ECO:0000256|ARBA:ARBA00010719,
CC       ECO:0000256|PIRNR:PIRNR036511}.
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DR   EMBL; KQ954569; KWU41037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FAT6; -.
DR   STRING; 1305733.A0A109FAT6; -.
DR   OrthoDB; 536at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd06100; CCL_ACL-C; 1.
DR   Gene3D; 3.30.470.110; -; 1.
DR   Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR   Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR014608; ATP-citrate_synthase.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR032263; Citrate-bd.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF16114; Citrate_bind; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF036511; ATP_citrt_syn; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036511};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR036511};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR036511};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR036511};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR036511};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR036511};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR036511};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT   DOMAIN          539..648
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   ACT_SITE        807
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ   SEQUENCE   1135 AA;  123123 MW;  72C60AAED77AB8BF CRC64;
     MSSKPIREYD AKLLVAYHLG RAPNVGTKAV ARESFTSTPV KVAQVSWDPE TKQITDDATL
     PHWVFTEKLV AKPDQLIKRR GKAGLLALNK TWDEAKQWIS ERAGKQVQVE KTTGTLNNFI
     VEPMCPHPDD SEYYICINSV REGDVILFTH EGGVDVGDVD AKALTLTVPV GGELPTREEI
     KASLLKHVAG GERQDALVDF IIRLYAVYVD LHFAYLEINP LVAVENPSTG KTDIFYLDMA
     AKLDQTAEFI VGPKWAIARD PSVVNPGAAA ANGNGRISAD KGPPMFWPPP FGRDLTKEEA
     YIAKLDASTG ASLKLTVLNP EGRVWTMVAG GGASVVYSDA IAAHGFAHEL ANYGEYSGAP
     TTTQTYEYAK TILDLMTRGT PRPDGKILFI GGGIANFTNV AATFKGIISA LKEYQHRLQE
     HKVRIFVRRG GPNYQEGLKA MRLLGETLGV EIQVFGPDSH ITAIVPLGLG ITKAQPAALK
     AVNGAGPLDG NLTPVTPGSP KQSNISIVDS SREQPQDRIV DFSDKVHAAS ESGRPWFRPF
     DETTRSIVFG LQPRAIQGML DFDFACGRET PSVAAMVYPF GGHHIQKFYW GTKETLLPVY
     TSMKEAVAKC PDADVVVNFA SSRSVYQSTL EALEFPQIKA IALIAEGVPE RHAREILHAA
     QQKKVIIIGP ATVGGIKPGC FRIGNTGGMI DNILSSKLYR AGSVGYVSKS GGMSNELNNI
     LALTTDGTYE GIAIGGDRYP GTTFIDHLLR YEADPNCKLL VLLGEVGGIE EYRVIEAVKA
     GVIKKPIIAW AIGTCAKMFT TDVQFGHAGS MANSDLETAE AKNNAMRAAG FIVPPTFEDL
     PEVLAETYKK LVSAGTIVPK PEVPPPTIPM DYKWAQELGM IRKPAAFIST ISDERGQELL
     YAGMPISDVF KEDIGVGGVL SLLWFKRRLP AYATKFLEMV LMLTADHGPA VSGAMTTVIT
     ARAGKDLVSS LVAGLLTIGD RFGGALDGAA AEFTRAYESG MSPREFVDSM RKANKLIPGI
     GHKIKSKANP DKRVELVKKY VFEHFPSTKM LEYALAVEEV TSAKKDTLIL NVDGCLGVVF
     VDLLKYSGAF TMEEAGEYLK ATLNGLFVLG RSIGFIGHFI DQKRLKQPLY RHPAE
//
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