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Database: UniProt
Entry: A0A1V6YF79_PENNA
LinkDB: A0A1V6YF79_PENNA
Original site: A0A1V6YF79_PENNA 
ID   A0A1V6YF79_PENNA        Unreviewed;       655 AA.
AC   A0A1V6YF79;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-NOV-2023, entry version 23.
DE   RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE            EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN   ORFNames=PENNAL_c0022G01941 {ECO:0000313|EMBL:OQE86126.1},
GN   PNAL_LOCUS2957 {ECO:0000313|EMBL:CAG8039199.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE86126.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|EMBL:OQE86126.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE86126.1};
RA   Nielsen J.C., Nielsen J.;
RT   "Uncovering the secondary metabolism of Penicillium species provides
RT   insights into the evolution of 6-MSA pathways.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
RN   [3] {ECO:0000313|EMBL:CAG8039199.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Branca A.L. A.;
RL   Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE86126.1}.
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DR   EMBL; CAJVNV010000099; CAG8039199.1; -; Genomic_DNA.
DR   EMBL; MOOB01000022; OQE86126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6YF79; -.
DR   STRING; 60175.A0A1V6YF79; -.
DR   OMA; PKIPMDY; -.
DR   OrthoDB; 536at2759; -.
DR   Proteomes; UP000191691; Unassembled WGS sequence.
DR   Proteomes; UP001153461; 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: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; 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; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
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; PF00285; Citrate_synt; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          36..145
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   655 AA;  71558 MW;  7B7F67157DEC23C5 CRC64;
     MPSSTLPAGN GVQSANDNIT RFAPPSRVLT PAQHSLFHNK TRCFVYGMQP RAVQGMLDFD
     FICKRSTPSV AGIIYTFGGQ FVSKMYWGTS ETLLPVYQDV EKAMAKHPDV DTVVNFASSR
     SVYSSTMELM ENPQIRSIAI IAEGVPERRA REIMVTAKEK GITIIGPATV GGIKPGAYKI
     GNTGGMMDNI VASKLYRKGS VGYVSKSGGM SNELNNIISQ NTDGVFEGVA IGGDRYPGTT
     FIDHLLRYQA ESECKILVLL GEVGGVEEYR VIEAIKNGTI TKPVVAWAIG TCASMFKTEV
     QFGHAGASAN SDLETAVTKN KAMREAGIHV PETFEDLPQM LKQVYDAELQ KGNITPAPEP
     IVPKIPIDYS WAQELGLVRK PAAFISTISD DRGQELLYAG MPISDVFRED IGIGGVMSLL
     WFRRRLPTYA SKFLEMVLML TADHGPAVSG AMNTIITTRA GKDLISALVS GLLTIGSRFG
     GALDGAAEEF TKAFDKGLSP RDFVDTMRKE NKLIPGIGHK VKSRNNPDLR VELVKEFVKK
     HFPSTKLLDY AIAVETVTTS KKDNLILNVD GCIAVCFVDL LRNCGAFSPE ECEDYMRMGV
     LNGLFVLGRS IGLIAHYLDQ KRLRTGLYRH PWDDITYLLP TLQKGGAEGR VEVNL
//
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