ID A0A2A2EH58_9BIFI Unreviewed; 431 AA.
AC A0A2A2EH58;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN ORFNames=B1526_0502 {ECO:0000313|EMBL:PAU68317.1};
OS Bifidobacterium criceti.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1960969 {ECO:0000313|EMBL:PAU68317.1, ECO:0000313|Proteomes:UP000218399};
RN [1] {ECO:0000313|EMBL:PAU68317.1, ECO:0000313|Proteomes:UP000218399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71 {ECO:0000313|EMBL:PAU68317.1,
RC ECO:0000313|Proteomes:UP000218399};
RX PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT tree of life.";
RL ISME J. 11:2834-2847(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;
CC Evidence={ECO:0000256|ARBA:ARBA00000308};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000256|ARBA:ARBA00004751}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAU68317.1}.
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DR EMBL; MVOH01000006; PAU68317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2EH58; -.
DR OrthoDB; 9800864at2; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000218399; Unassembled WGS sequence.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.20.28.60; -; 1.
DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 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; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR42871; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR42871:SF1; CITRATE SYNTHASE; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; Citrate synthase; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|PIRNR:PIRNR001369}.
FT ACT_SITE 302
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 365
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 431 AA; 48542 MW; AE279AB8E383A02B CRC64;
MGVAQLHVES NQFELPVVKA SAGPDGIVMS SLRNDNWVSL DPGFLTTAQC ESKITYIDGE
HSILRYRGYP IEQLCEQSDF LEVSWLLRNG ELPTRAQYER FVDDINHHTM VGEDFRTFMG
AFPREAQPMS VMASAINALA TFNPDTTDIC DPDQLDEAAT IIMAKARTVV SYILRRRRDE
PMLYPDYARG YVDDFLRMCF AVPYEQFESD PLYVHALGRL LIIHADHEQN CSTSVVRIAG
SAHANLYSAV AAGINALSGP LHGGANEAVL RQLMAIRDSG MSVREFVDRA KLNGDRISGL
GHRVYKSYDP RAAIAKHYLE RIMEQTATLK LLPGDEELFD VALQLEDIAL HDDYFVSRHL
YPNVDFYTGL IYRAIGFGPS MFTPLFALGR IPGWIAQYRE MLADPMTKIG RPRQVYTGEV
LRDYVPIDER G
//