ID A0A165F6C4_9BASI Unreviewed; 1152 AA.
AC A0A165F6C4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CALCODRAFT_497597 {ECO:0000313|EMBL:KZT56281.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT56281.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT56281.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT56281.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV423980; KZT56281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165F6C4; -.
DR STRING; 1353952.A0A165F6C4; -.
DR InParanoid; A0A165F6C4; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000076842; 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; 1.10.230.10; 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; 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|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}; Magnesium {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:UP000076842};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036511}.
FT DOMAIN 536..645
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 804
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1152 AA; 125734 MW; A7004B0D3C3E536E CRC64;
MSSKAIREFD AKLLLAYWLE RSPSVSPSAK ISPGFVYPAP HVAQISWDPE TGAITPDSQL
PPWVFTSKLV AKPDQLIKRR GKAGLLLLNK EWPEAKEWIA ARAGKDVTVS STTGKLSNFI
VEPFLPHPSH TEYYVCINSV REGDNILFTH EGGIEVGDVD AKALKLLIPV GKEFPSRDAI
KKALLTHVPE EKKDTLVDFL IRLYSVYVDL HFAYLEINPL ICLDGVNGKP PTIHYLDMAA
KLDQTADYLC GPKWAIARDL SVYDSRAQSN GIMADRGPPM VWPAPFGRDL TKEEAYIQKL
DGSTGASLKL TVLNANGRIW TMVAGGGASV VYSDAIAAAG FAHELANYGE YSGAPTEGQT
YEYAKTIIDL ITRGAPRPDG KILIIGGGIA NFTNVAATFK GIIRALKEYK APLINHKVQI
YIRRGGPNYQ EGLKAMRLLG ESLGVPIHVF GPETHITAIV PLALGLVKEA QQVTATIANG
IHEDDGTGKG SIQGEVQVDE DQPVGPIGPS GERTQPNDKI VHFDFHASAK RPWFRPFDAS
TRSLVFGLQP RAIQGMLDFD YSCGRQTPSV AAMIYPFGGH HIQKFYWGTK ETLLPVYTST
EEAVKKHPDA DVVVNFASSR SVYQSTMEML ALPQIKAIAI IAEGVPERYA REILHLAEEK
HVLIIGPATV GGIKPGCFRI GNSGGMMDNI IASKLYRPGS VGYVSKSGGM SNELNNILSL
VTNGTYEGIA IGGDRYPGTT FIDHMLRYEA DPECKMLVLL GEVGGIEEYR VIEAVKSGKI
TKPIVAWAIG TCAKMFTTEV QFGHAGSMAN SDLETADAKN AAMKAAGFIV PDTFEELPTV
LTETYRKLVK SGVIKVTAER EPPVIPMDYK WAQELGLIRK PAAFISTISD ERGQELMYAG
MRISDVFKED IGIGGVVSLL WFKRRLPPYA TKFIEMVLML TADHGPAVSG AMNTIVATRA
GKDLISSLAS GLLTIGSRFG GALDEAAAMF SEAKDTGLTP REFVDQCRKK NKLISGIGHK
IKSVNNPDLR VELVKEFVQK NFPTHTLLDY ALAVEKVTTA KKDTLILNVD GCIAVCFVDL
LRDSGAFSRE EADEYIRIGT LNGLFVCGRS IGFIGHHLDQ KRLRAPLYRH PADDIFINMQ
DMSQPRVLAK TA
//
