CISY_ACEAC
ID CISY_ACEAC Reviewed; 436 AA.
AC P20901;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
DE AltName: Full=Acetic acid resistance protein;
GN Name=aarA;
OS Acetobacter aceti.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX NCBI_TaxID=435;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2156811; DOI=10.1128/jb.172.4.2096-2104.1990;
RA Fukaya M., Takemura H., Okumura H., Kawamura Y., Horinouchi S., Beppu T.;
RT "Cloning of genes responsible for acetic acid resistance in Acetobacter
RT aceti.";
RL J. Bacteriol. 172:2096-2104(1990).
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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homohexamer.
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; M34830; AAA21883.1; -; Genomic_DNA.
DR PIR; A35157; YKQPC.
DR PDB; 2H12; X-ray; 1.85 A; A/B/C/D/E/F=1-436.
DR PDBsum; 2H12; -.
DR AlphaFoldDB; P20901; -.
DR SMR; P20901; -.
DR PRIDE; P20901; -.
DR BioCyc; MetaCyc:MON-17983; -.
DR BRENDA; 2.3.3.16; 33.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; P20901; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd06114; EcCS_like; 1.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
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 InterPro; IPR010953; Citrate_synthase_typ-I.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01798; cit_synth_I; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..436
FT /note="Citrate synthase"
FT /id="PRO_0000169923"
FT ACT_SITE 313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2H12"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:2H12"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2H12"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:2H12"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2H12"
FT STRAND 57..68
FT /evidence="ECO:0007829|PDB:2H12"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:2H12"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 165..188
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:2H12"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:2H12"
FT TURN 270..274
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 321..336
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 388..409
FT /evidence="ECO:0007829|PDB:2H12"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:2H12"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:2H12"
SQ SEQUENCE 436 AA; 48197 MW; 3E6F0DD5D4216244 CRC64;
MSASQKEGKL STATISVDGK SAEMPVLSGT LGPDVIDIRK LPAQLGVFTF DPGYGETAAC
NSKITFIDGD KGVLLHRGYP IAQLDENASY EEVIYLLLNG ELPNKVQYDT FTNTLTNHTL
LHEQIRNFFN GFRRDAHPMA ILCGTVGALS AFYPDANDIA IPANRDLAAM RLIAKIPTIA
AWAYKYTQGE AFIYPRNDLN YAENFLSMMF ARMSEPYKVN PVLARAMNRI LILHADHEQN
ASTSTVRLAG STGANPFACI AAGIAALWGP AHGGANEAVL KMLARIGKKE NIPAFIAQVK
DKNSGVKLMG FGHRVYKNFD PRAKIMQQTC HEVLTELGIK DDPLLDLAVE LEKIALSDDY
FVQRKLYPNV DFYSGIILKA MGIPTSMFTV LFAVARTTGW VSQWKEMIEE PGQRISRPRQ
LYIGAPQRDY VPLAKR
