CISY_HALVD
ID CISY_HALVD Reviewed; 379 AA.
AC D4GS06; O32705;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
GN Name=citZ; OrderedLocusNames=HVO_0466; ORFNames=C498_16349;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DS2 / DSM 5716 / WFD11;
RX PubMed=10397837;
RX DOI=10.1002/(sici)1097-0290(19990705)64:1<38::aid-bit4>3.0.co;2-7;
RA Connaris H., Chaudhuri J.B., Danson M.J., Hough D.W.;
RT "Expression, reactivation, and purification of enzymes from Haloferax
RT volcanii in Escherichia coli.";
RL Biotechnol. Bioeng. 64:38-45(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4]
RP PROTEIN SEQUENCE OF 2-39.
RX PubMed=1321743; DOI=10.1042/bst020012s;
RA James K.D., Bonete M.J., Byrom D., Danson M.J., Hough D.W.;
RT "Citrate synthase from Haloferax volcanii: enzyme purification and gene
RT cloning.";
RL Biochem. Soc. Trans. 20:12S-12S(1992).
CC -!- FUNCTION: Might regulate the synthesis and function of enzymes involved
CC in later enzymatic steps of Krebs cycle. {ECO:0000250}.
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:10397837};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=125 uM for acetyl-CoA {ECO:0000269|PubMed:10397837};
CC KM=26 uM for oxaloacetate {ECO:0000269|PubMed:10397837};
CC Vmax=36 umol/min/mg enzyme {ECO:0000269|PubMed:10397837};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: When expressed in E.coli, CitZ is produced in a soluble
CC but inactive form that can be reactivated by incubating with 2 M KCl
CC (PubMed:10397837). Citrate synthase is found in nearly all cells
CC capable of oxidative metabolism. {ECO:0000305|PubMed:10397837}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; AJ002075; CAA05174.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03756.1; -; Genomic_DNA.
DR EMBL; AOHU01000100; ELY25937.1; -; Genomic_DNA.
DR PIR; T44615; T44615.
DR RefSeq; WP_004044456.1; NZ_AOHU01000100.1.
DR AlphaFoldDB; D4GS06; -.
DR SMR; D4GS06; -.
DR STRING; 309800.C498_16349; -.
DR EnsemblBacteria; ADE03756; ADE03756; HVO_0466.
DR EnsemblBacteria; ELY25937; ELY25937; C498_16349.
DR GeneID; 8925804; -.
DR KEGG; hvo:HVO_0466; -.
DR PATRIC; fig|309800.29.peg.3168; -.
DR eggNOG; arCOG04237; Archaea.
DR HOGENOM; CLU_025068_2_1_2; -.
DR OMA; NEAVMHM; -.
DR OrthoDB; 39666at2157; -.
DR BRENDA; 2.3.3.16; 2561.
DR SABIO-RK; D4GS06; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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; 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.
PE 1: Evidence at protein level;
KW Acyltransferase; Allosteric enzyme; Direct protein sequencing;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:1321743"
FT CHAIN 2..379
FT /note="Citrate synthase"
FT /id="PRO_0000428843"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /evidence="ECO:0000250"
FT ACT_SITE 316
FT /evidence="ECO:0000250"
FT CONFLICT 264
FT /note="G -> V (in Ref. 1; CAA05174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 41807 MW; 6F33615AAF4E0BDD CRC64;
MSGELKRGLE GVLVAESKLS FIDGDAGQLV YCGYDIEDLA RDASYEEVLY LLWHGALPTG
EELDAFSDEL AAHRDLDDGV LDVARELAEQ DESPMAALRT LVSAMSAYDE SADFEDVTDR
EVNLEKAKRI TAKMPSVLAA YARFRRGDDY VEPDESLNHA ANFLYMLNGE EPNEVLAETF
DMALVLHADH GLNASTFSAM VTSSTLSDLY SAVTSAIGTL SGSLHGGANA NVMRMLKDVD
DSDMDPTEWV KDALDRGERV AGFGHRVYNV KDPRAKILGA KSEALGEAAG DMKWYEMSVA
IEEYIGEEKG LAPNVDFYSA STYYQMGIPI DLYTPIFAVS RAGGWIAHVL EQYEDNRLIR
PRARYTGEKD LDFTPVDER