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Database: UniProt
Entry: A0A1Q7URJ4_9CHLR
LinkDB: A0A1Q7URJ4_9CHLR
Original site: A0A1Q7URJ4_9CHLR 
ID   A0A1Q7URJ4_9CHLR        Unreviewed;       373 AA.
AC   A0A1Q7URJ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN   ORFNames=AUG82_04125 {ECO:0000313|EMBL:OLE06093.1};
OS   Ktedonobacter sp. 13_1_20CM_4_53_11.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE06093.1, ECO:0000313|Proteomes:UP000186213};
RN   [1] {ECO:0000313|EMBL:OLE06093.1, ECO:0000313|Proteomes:UP000186213}
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:OLE06093.1}.
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DR   EMBL; MNIY01000081; OLE06093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7URJ4; -.
DR   STRING; 1805225.AUG82_04125; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000186213; 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;  41711 MW;  BE5246DF2CBB8F1E CRC64;
     MPTTDGLEDI VATNSRICDL DGKLGKLTYY GVDIHDLARY SSFEETAYLL WHGILPTRAQ
     LEEVTAQLQA NRELPGRVIE IMHLLPRSSS PMEVLRTIVS TLSSFDPNPE DRSPGANYGR
     AIRLTAALGT IVTSWEHIRN GMKPVAPLPD HNTATNFLYM LNGEMPDDYT AHALDTALVL
     HADHELNAST FAARVTAGTL ADMYASITSA IGALSGPLHG GANEQVMRML LRIGEVSNTE
     PYIRNAVEHK ERIMGFGHRV YKTEDPRATH LRAMSEELGK RTGDSRWFKM SRIIEDYIKE
     QKGLYCNVDF YSASVYYMLG FPIDLDTPIF ACSRIAGYTA HVLEQYANNR LIRPRAEYVG
     PKVTQYVPIE QRG
//
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