CISY_THET7
ID CISY_THET7 Reviewed; 442 AA.
AC A0A0S3QTD0;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Citrate synthase {ECO:0000303|PubMed:29420286};
DE Short=CS {ECO:0000303|PubMed:29420286};
DE EC=2.3.3.16 {ECO:0000269|PubMed:29420286};
GN Name=gltA {ECO:0000312|EMBL:BAT71583.1};
GN ORFNames=TST_0783 {ECO:0000312|EMBL:BAT71583.1};
OS Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 /
OS ABI70S6).
OC Bacteria; Aquificae; Aquificales.
OX NCBI_TaxID=1298851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6;
RX PubMed=29420286; DOI=10.1126/science.aao3407;
RA Nunoura T., Chikaraishi Y., Izaki R., Suwa T., Sato T., Harada T., Mori K.,
RA Kato Y., Miyazaki M., Shimamura S., Yanagawa K., Shuto A., Ohkouchi N.,
RA Fujita N., Takaki Y., Atomi H., Takai K.;
RT "A primordial and reversible TCA cycle in a facultatively
RT chemolithoautotrophic thermophile.";
RL Science 359:559-563(2018).
CC -!- FUNCTION: Catalyzes both citrate generation and citrate cleavage. Part
CC of a reversible tricarboxylic acid (TCA) cycle that can fix carbon
CC dioxide autotrophically and may represent an ancestral mode of the
CC conventional reductive TCA (rTCA) cycle. The direction is controlled by
CC the available carbon source(s). {ECO:0000269|PubMed:29420286}.
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;
CC Evidence={ECO:0000269|PubMed:29420286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16846;
CC Evidence={ECO:0000269|PubMed:29420286};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16847;
CC Evidence={ECO:0000269|PubMed:29420286};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.6 uM for citrate {ECO:0000269|PubMed:29420286};
CC KM=17.4 uM for CoA {ECO:0000269|PubMed:29420286};
CC KM=41.2 uM for oxaloacetate {ECO:0000269|PubMed:29420286};
CC KM=56.3 uM for acetyl-CoA {ECO:0000269|PubMed:29420286};
CC Vmax=1.11 umol/min/mg enzyme toward citrate for the reverse reaction
CC {ECO:0000269|PubMed:29420286};
CC Vmax=1.60 umol/min/mg enzyme toward CoA for the reverse reaction
CC {ECO:0000269|PubMed:29420286};
CC Vmax=298 umol/min/mg enzyme toward acetyl-CoA for the forward
CC reaction {ECO:0000269|PubMed:29420286};
CC Note=kcat is 0.931 sec(-1) with citrate as substrate. kcat is 1.34
CC sec(-1) with CoA as substrate. kcat is 250 sec(-1) with acetyl-CoA as
CC substrate. {ECO:0000269|PubMed:29420286};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000269|PubMed:29420286}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; AP013035; BAT71583.1; -; Genomic_DNA.
DR RefSeq; WP_068549585.1; NZ_AP013035.1.
DR AlphaFoldDB; A0A0S3QTD0; -.
DR SMR; A0A0S3QTD0; -.
DR STRING; 1298851.TST_0783; -.
DR EnsemblBacteria; BAT71583; BAT71583; TST_0783.
DR KEGG; ttk:TST_0783; -.
DR PATRIC; fig|1298851.3.peg.818; -.
DR OMA; NEAVMHM; -.
DR OrthoDB; 1412360at2; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000063234; Chromosome.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..442
FT /note="Citrate synthase"
FT /id="PRO_0000443956"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:P21553"
FT ACT_SITE 320
FT /evidence="ECO:0000250|UniProtKB:P21553"
FT ACT_SITE 375
FT /evidence="ECO:0000250|UniProtKB:P21553"
SQ SEQUENCE 442 AA; 50337 MW; 31C9DB506137CB93 CRC64;
MKLKERLAEL IPQWRAEVAE IRKKYGNRKT MDCTIGHAYG GMRGLKALVC DTSEVFPDEG
VKFRGYTIPE LREGPHKLPT AEGGFEPLPE GLWYLLLTGE LPTEEDVKEI SAEFTKRMQN
VPQYVFDVLR AMPVDTHPMT MFAAGILAMQ RESVFAKRYE EGMRREEHWE AMLEDSLNML
AALPVIAAYI YRRKYKGDTH IAPDPNLDWS ANLAHMMGFD DFEVYELFRL YMFLHSDHEG
GNVSAHTNLL VNSAYSDIYR SFSAAMNGLA GPLHGLANQE VLRWIQMLYK KFGGVPTKEQ
LERFAWDTLN SGQVIPGYGH AVLRVTDPRY VAQRDFALKH LPDDELFKIV SLCYEVIPEV
LKKHGKAKNP WPNVDAHSGV LLWHYGIREY DFYTVLFGVS RALGCTAQAI LVRGYMLPIE
RPKSITTRWV KEVAESLPVA GS
