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Database: UniProt
Entry: A6R5M6_AJECN
LinkDB: A6R5M6_AJECN
Original site: A6R5M6_AJECN 
ID   A6R5M6_AJECN            Unreviewed;       659 AA.
AC   A6R5M6;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE            EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN   ORFNames=HCAG_04934 {ECO:0000313|EMBL:EDN08435.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08435.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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DR   EMBL; CH476659; EDN08435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6R5M6; -.
DR   STRING; 339724.A6R5M6; -.
DR   VEuPathDB; FungiDB:HCAG_04934; -.
DR   HOGENOM; CLU_006587_4_1_1; -.
DR   OMA; HMLRYQA; -.
DR   OrthoDB; 536at2759; -.
DR   Proteomes; UP000009297; 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; 1.10.580.10; 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; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
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; 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; PF00285; Citrate_synt; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
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:UP000009297};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          38..147
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   659 AA;  71747 MW;  24E751F9D64C0295 CRC64;
     MPSAAPLAST SNGNLSANDN IRRFAAPSRP FTPLEHSLFH NKTRCFVYGM QPRAVQGMLD
     FDFICKRTTP SVAGIIYTFG GQFVSKMYWG TSETLLPVYQ AVGKAIAKHP DVDTVVNFAS
     SRSVYSSTME LMQYPQIKSI AIIAEGVPER RAREIMVAAK EKGITIIGPA TVGGIKPGAF
     KIGNTGGMMD NIVASKLYRK GSVGYVSKSG GMSNELNNII SQTTDGVYEG VAIGGDRYPG
     TTFIDHLLRY QADPECKILV LLGEVGGVEE YRVIEAVRDG TITKPVVAWA IGTCASLFKT
     EVQFGHAGAS ANSELETAVM KNKCMREAGI HVPETFEELP QTLAEVYKKL VKQGTIVPQS
     EPVPPKIPID YAWAQELGLI RKPAAFISTI SDDRGQELLY AGMPISDVFR EDIGIGGVMS
     LLWFRRRLPN YASKFLEMVL MLTADHGPAV SGAMNTIITT RAGKDLISAL VSGLLTIGSR
     FGGALDGAAE EFTKAFDKGL SPRDFVDTMR KENKLIPGIG HKVKSRANPD LRVELVKEFV
     HKNFPSHKLL DYAIAVETVT TSKKDNLILN VDGCVAVCFV DLLRNCGAFS PEEAEDYLSM
     GVLNGLFVLG RSIGLIAHFL DQKRLRTGLY RHPWDDITYL LPSFQKGAPG AEGRVEVSL
//
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