ID A0A0B7NI96_9FUNG Unreviewed; 1177 AA.
AC A0A0B7NI96;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
DE AltName: Full=ATP-citrate (pro-S-)-lyase {ECO:0000256|ARBA:ARBA00030151};
DE AltName: Full=Citrate cleavage enzyme {ECO:0000256|ARBA:ARBA00030982};
GN Name=PARPA_11424.1 scaffold 44101 {ECO:0000313|EMBL:CEP17132.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP17132.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP17132.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP17132.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000256|ARBA:ARBA00005899}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000256|ARBA:ARBA00010719}.
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DR EMBL; LN733608; CEP17132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NI96; -.
DR STRING; 35722.A0A0B7NI96; -.
DR OrthoDB; 536at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
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; IPR017866; Succ-CoA_synthase_bsu_CS.
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 PRINTS; PR01798; SCOASYNTHASE.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 302..479
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
FT DOMAIN 552..658
FT /note="CoA-binding"
FT /evidence="ECO:0000259|Pfam:PF02629"
FT DOMAIN 718..842
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT ACT_SITE 818
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036511-1"
SQ SEQUENCE 1177 AA; 129882 MW; 82FC5E88395F332B CRC64;
MSAKPIREYD GKLLLAYHLL RAPPVGKQQD TISLFTPAAT KLAHINVNTS LSGDEAAFKS
ALKQQLDNLE QTHPWLLTDK LVAKPDQLIK RRGKHGLLAL NKDWADARKW IEERAGKEIK
IERTTGVLKT FLVEPFAPHP DNTEYYICIN SVREGDYILF THEGGIEVGD VDAKALKLLI
PVSSADFPSA DTIKQTLLKD VPEFKRDVLV DFIRRLYAVY VDLHFTYLEI NPLVVTDPVE
GHTPQVMYLD LAAKIDQTAE FEAGPKWAVA RAPQNIGLVP SGSDAQNVDQ GPPMDFPAPF
GRELTREEAY IQELDGKTGA SLKLTVLNRD GRIWTMVAGG GASVVYSDAI AALGYADELA
NYGEYSGAPT ETQTYEYAKT ILDLMTRGDV NSQGKLLFIG GGIANFTNVA TTFKGIIRAL
TEFKQALINH KVRIFIRRGG PNYQEGLRAM RQLGETLGVE IQVFGPETHI TEIVPLALEG
KATSLQSGPS AASGNLFQDQ IFGSNTNSGA NTPKLTIAED NQTPTNPNER MTYFPEQEGQ
EESAEWYRPF TSKTRAFVYG MQPRAVQGML DFDFMCKRET PSVAAMVYPF GGSHVQKFYW
GTKETLIPVF TSLKEAIEQF PEVDVVVNFA SCRSVFDSTR EIFAFSEQIK TIAIIAEGVP
ERRARQLLHE AEARKVLVIG PATVGGIKPG CFKIGNTGGM MDNIVSSKLY RAGSVGYVSK
SGGMSNELNN IVSRTTDGVY EGVAIGGDRY PGSTFIDHLL RYEEDPNCKM LVLLGEVGGI
EEYRVIEAVQ NGTIKKPIVA WCIGTCAKMF TTDVQFGHAG SMANSDLETA DTKNKAMRAA
GIIVPETFEK MPLALAETYT KLVKEGVIHP RAEPEIPKIP IDYSWAQELG LVRKPASFVS
TIVDDRGQEL LYAGMRITDV FKEDVGIGGV LSLLWFKRRL PNYACKFIEM VLMLTADHGP
AVSGAMNTII TTRAGKDLIS SLVSGLLTIG ERFGGALDGA ASNFTKAYDS GMTPREFVTS
MRKANKLIPG IGHKIKSRTN PDMRVELVKD YVKKNFPHTP ILDYALKVEE ITTSKKDNLI
LNVDGCIAVS FVDLLRESGA FTHDEAEEYM RIGTLNGLFV LGRSLGFIGH HLDQKRLKQG
LYRHPWDDIS YLLPSLDPET LDPRRVNARV NVQPKQQ
//
