UniProt: A0A1B7NEN8

Database: UniProt
Entry: A0A1B7NEN8_9AGAM

LinkDB:  A0A1B7NEN8_9AGAM 
Original site:  A0A1B7NEN8_9AGAM

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (19)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (2)   
   SMART (1)   
All databases (30)   

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ID   A0A1B7NEN8_9AGAM        Unreviewed;      1154 AA.
AC   A0A1B7NEN8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=K503DRAFT_681679 {ECO:0000313|EMBL:OAX43220.1};
OS   Rhizopogon vinicolor AM-OR11-026.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX43220.1, ECO:0000313|Proteomes:UP000092154};
RN   [1] {ECO:0000313|EMBL:OAX43220.1, ECO:0000313|Proteomes:UP000092154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX43220.1,
RC   ECO:0000313|Proteomes:UP000092154};
RG   DOE Joint Genome Institute;
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (JUN-2016) 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|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|PIRNR:PIRNR036511}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC       CoA ligase beta subunit family. {ECO:0000256|PIRNR:PIRNR036511}.
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DR   EMBL; KV448142; OAX43220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7NEN8; -.
DR   STRING; 1314800.A0A1B7NEN8; -.
DR   InParanoid; A0A1B7NEN8; -.
DR   OrthoDB; 536at2759; -.
DR   Proteomes; UP000092154; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 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.
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}; Lyase {ECO:0000313|EMBL:OAX43220.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR036511};
KW   Metal-binding {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:UP000092154};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT   DOMAIN          538..647
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   REGION          473..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        806
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ   SEQUENCE   1154 AA;  125325 MW;  3B31B73499924E63 CRC64;
     MSSKAIREYD AKLLLAYWLQ RAPSPNPNFD ISPSSTLQFP APRVAQIQWE PATDTITPDS
     LLPSWVSTTK LVAKPDQLIK RRGKAGLLAL NKEWPDAKKW IVERAGKPQR VESVTGTLSS
     FIVEPFLPHP SDSEYYICIT SARHADTLLF TTSGGVDVGD VDAKALKLDI PVLGPFPTRA
     ELQNTLLRDV PKHKKEVLTD FLVRLYAVYV DLHFAYLEIN PLVVLDDGSI HYLDMAAKLD
     QTAESICGPK WAVARDLTVY ETGPAVSTTT SKVTADRGPP MAWPAPFGRD LTKEEAYIQK
     LDASTGASLK LTVLNPTGRI WTMVAGGGAS VVYSDAIAAA GFAHELANYG EYSGAPTEGQ
     TFEYAKTILD LITRPPPRAD GKILIIGGGI ANFTNVAATF KGIIRALTMF KAQLIAHRAK
     IYVRRGGPNW QEGLKAMRLL GESLGVPIHV FGPDTHITDV VPLALGLKSS TSSTAPVSLS
     ATAPGSPKVA TETPSGELDS SDVGTIHASG ERTQPNDVVV RFDAVNGSAK AARPAYRPFD
     EDTRSFVYGL QPRAIQGMLD FDYSCKRARP SVAAMIYPFG GHHIQKFYWG TRETLLPVYT
     SLEEAVKKHP DVDVVVNFAS SRSVYSSTME CLSHESIRAI ALIAEGVPER QAREILWKAQ
     AKGVLIIGPA TVGGIKPGCF RIGNSGGMMD NIIASKLYRP GSVGYVSKSG GMSNELNNIL
     SLVTNGTYEG IAIGGDRYPG STFIDHLLRY EADPACKMLV LLGEVGGVEE YRVIDAVKSG
     QIKKPIVAWA IGTCASMFTT EVQFGHAGSM ANSDSETAAA KNRAMREAGF IVPNTFEELP
     IALKETYERL VREGTIVPTR DVEPPVIPMD YKWAQELGLI RKPAAFISTI SDERGQELLY
     AGMRISDVFK EDIGLGGVVS LLWFKRRLPS WATKFIEMVL MLTADHGPAV SGAMNTIVAT
     RAGKDLISSL ASGLLTIGSR FGGALDEAAS MFSGARDTGL TPREFVDNSR KANKLISGIG
     HKIKSVNNPD LRVELVKEYV RKNFPSHSLL DYALAVEKVT TSKKDTLILN VDGCIAVCFV
     DLLRDSGAFT PEEAEEYIKI GTLNGLFVLG RSIGFIGHHL DQKRLRAPLY RHPADDIFIN
     IADLSQPRVL GKMQ
//

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