ID A0A1Q7IES4_9CHLR Unreviewed; 373 AA.
AC A0A1Q7IES4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN ORFNames=AUH89_01620 {ECO:0000313|EMBL:OLC62162.1};
OS Ktedonobacter sp. 13_1_40CM_4_52_4.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805230 {ECO:0000313|EMBL:OLC62162.1, ECO:0000313|Proteomes:UP000186693};
RN [1] {ECO:0000313|EMBL:OLC62162.1, ECO:0000313|Proteomes:UP000186693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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.
CC {ECO:0000256|ARBA:ARBA00005163}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369,
CC ECO:0000256|RuleBase:RU003406}.
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:OLC62162.1}.
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DR EMBL; MNFP01000031; OLC62162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7IES4; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000186693; 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 CDD; cd06110; BSuCS-II_like; 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; 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; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR NCBIfam; TIGR01800; cit_synth_II; 1.
DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR11739:SF4; CITRATE SYNTHASE, PEROXISOMAL; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; Citrate synthase; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369}.
FT ACT_SITE 258
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 309
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 373 AA; 42149 MW; 6DD428546C54BA4A CRC64;
MSTTDGLEDI VATHSRICDL DGKLGKLTYF GVDIHDLARY STFEETAYLL WHGVLPTRTQ
LEEVSALLQA NRELPGRVIE IMHLLPRTTP AMDVLRTIVS TLSSFDPNPD DKSAEANYRR
AIRLTAVLGT IVTTWEHIRN GRKPVAPLRD HNTATNFLYM LKGEMPDEYT AHVFDVALVL
HADHELNAST FAARVTAGTL ADMYASITSA IGALSGPLHG GANEQVMRML LRIGEVSNAE
PYIRDAVERK ERIMGFGHRV YKTEDPRATH LREMSKEMGI HNGDSRWYEM SRIIEDYIKE
HKGLYCNVDF YSASVYYMMG IPIDLDTPVF ARSRIAGYTA HVLEQYSNNR LIRPRAEYVG
PKVTEYIPIE QRG
//