CISY_SACS2
ID CISY_SACS2 Reviewed; 377 AA.
AC P80148; P77979;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 3.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
GN Name=gltA; OrderedLocusNames=SSO2589;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1;
RA Connaris H., Danson M.J., Hough D.W.;
RT "Sulfolobus solfataricus citrate synthase.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP PROTEIN SEQUENCE OF 7-30, AND ACETYLATION.
RX PubMed=1521537; DOI=10.1111/j.1432-1033.1992.tb17208.x;
RA Lill U., Lefrank S., Henschen A., Eggerer H.;
RT "Conversion, by limited proteolysis, of an archaebacterial citrate synthase
RT into essentially a citryl-CoA hydrolase.";
RL Eur. J. Biochem. 208:459-466(1992).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by NADH.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer.
CC -!- PTM: The N-terminus is blocked by acetylation.
CC {ECO:0000269|PubMed:1521537}.
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; U70879; AAB09594.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42713.1; -; Genomic_DNA.
DR PIR; B90432; B90432.
DR RefSeq; WP_009989299.1; NC_002754.1.
DR PDB; 1O7X; X-ray; 2.70 A; A/B/C/D=1-377.
DR PDBsum; 1O7X; -.
DR AlphaFoldDB; P80148; -.
DR SMR; P80148; -.
DR STRING; 273057.SSO2589; -.
DR EnsemblBacteria; AAK42713; AAK42713; SSO2589.
DR GeneID; 44128319; -.
DR KEGG; sso:SSO2589; -.
DR PATRIC; fig|273057.12.peg.2670; -.
DR eggNOG; arCOG04237; Archaea.
DR HOGENOM; CLU_025068_2_1_2; -.
DR InParanoid; P80148; -.
DR OMA; NEAVMHM; -.
DR PhylomeDB; P80148; -.
DR BRENDA; 2.3.3.16; 6163.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; P80148; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
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; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Direct protein sequencing;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..377
FT /note="Citrate synthase"
FT /id="PRO_0000169977"
FT ACT_SITE 258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT CONFLICT 10
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="I -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="V -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="N -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="F -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..25
FT /note="EK -> VN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="I -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="P -> R (in Ref. 1; AAB09594)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1O7X"
FT STRAND 12..22
FT /evidence="ECO:0007829|PDB:1O7X"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:1O7X"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:1O7X"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 116..138
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:1O7X"
FT TURN 216..220
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:1O7X"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 283..303
FT /evidence="ECO:0007829|PDB:1O7X"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:1O7X"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1O7X"
FT HELIX 330..352
FT /evidence="ECO:0007829|PDB:1O7X"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1O7X"
SQ SEQUENCE 377 AA; 42752 MW; E3036E232F134F11 CRC64;
MSVVSKGLEN VIIKVTNLTF IDGEKGILRY RGYNIEDLVN YGSYEETIYL MLYGKLPTKK
ELNDLKAKLN EEYEVPQEVL DTIYLMPKEA DAIGLLEVGT AALASIDKNF KWKENDKEKA
ISIIAKMATL VANVYRRKEG NKPRIPEPSD SFAKSFLLAS FAREPTTDEI NAMDKALILY
TDHEVPASTT AALVAASTLS DMYSSLTAAL AALKGPLHGG AAEEAFKQFI EIGDPNRVQN
WFNDKVVNQK NRLMGFGHRV YKTYDPRAKI FKKLALTLIE RNADARRYFE IAQKLEELGI
KQFSSKGIYP NTDFYSGIVF YALGFPVYMF TALFALSRTL GWLAHIIEYV EEQHRLIRPR
ALYVGPEYQE YVSIDKR
