CISY2_MYCBO
ID CISY2_MYCBO Reviewed; 373 AA.
AC P63778; A0A1R3XWQ6; Q10529; X2BG39;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Putative citrate synthase 2;
DE EC=2.3.3.16;
GN Name=citA; OrderedLocusNames=BQ2027_MB0913C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; LT708304; SIT99511.1; -; Genomic_DNA.
DR RefSeq; NP_854570.1; NC_002945.3.
DR RefSeq; WP_003898633.1; NC_002945.4.
DR AlphaFoldDB; P63778; -.
DR SMR; P63778; -.
DR EnsemblBacteria; SIT99511; SIT99511; BQ2027_MB0913C.
DR PATRIC; fig|233413.5.peg.994; -.
DR OMA; YWTSAAE; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000001419; 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; -; 2.
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 3: Inferred from homology;
KW Allosteric enzyme; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..373
FT /note="Putative citrate synthase 2"
FT /id="PRO_0000169950"
FT ACT_SITE 250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ SEQUENCE 373 AA; 40147 MW; AABF5238CB79B54D CRC64;
MTVVPENFVP GLDGVVAFTT EIAEPDKDGG ALRYRGVDIE DLVSQRVTFG DVWALLVDGN
FGSGLPPAEP FPLPIHSGDV RVDVQAGLAM LAPIWGYAPL LDIDDATARQ QLARASVMAL
SYVAQSARGI YQPAVPQRII DECSTVTARF MTRWQGEPDP RHIEAIDAYW VSAAEHGMNA
STFTARVIAS TGADVAAALS GAIGAMSGPL HGGAPARVLP MLDEVERAGD ARSVVKGILD
RGEKLMGFGH RVYRAEDPRA RVLRAAAERL GAPRYEVAVA VEQAALSELR ERRPDRAIET
NVEFWAAVVL DFARVPANMM PAMFTCGRTA GWCAHILEQK RLGKLVRPSA IYVGPGPRSP
ESVDGWERVL TTA