ID A0A1Q8ATP3_9CREN Unreviewed; 375 AA.
AC A0A1Q8ATP3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU000441};
DE EC=2.3.3.16 {ECO:0000256|PIRNR:PIRNR001369};
GN ORFNames=AUF79_18775 {ECO:0000313|EMBL:OLE83131.1};
OS Crenarchaeota archaeon 13_1_20CM_2_51_8.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805093 {ECO:0000313|EMBL:OLE83131.1, ECO:0000313|Proteomes:UP000186073};
RN [1] {ECO:0000313|EMBL:OLE83131.1, ECO:0000313|Proteomes:UP000186073}
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|PIRNR:PIRNR001369};
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369,
CC ECO:0000256|RuleBase:RU000441}.
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:OLE83131.1}.
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DR EMBL; MNKD01000847; OLE83131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8ATP3; -.
DR Proteomes; UP000186073; Unassembled WGS sequence.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR11739:SF23; CITRATE SYNTHASE 2-RELATED; 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 255
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 309
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 375 AA; 41400 MW; 385715FA299B13E7 CRC64;
MIRAPKGLEG VIVATTSLTK IDGQAGRLIY RGYDVTQLAG RVSYESVAHL LWYGHLPNRQ
ELSTLETRFS REHVLPNQVI GFLKGESKVA DPLSALQTSV SILGGLGSRN EPSLIDSSIG
LTARMPTIVA TYHRLRKGQE PVTPRPGLGH AANYLYMLNA KPGRPEHVHA LDSYFTLLAD
HSLNASTFVA RIAASTLTDV HSAVVAAISA LKGPLHGGAP IYVWEMLQSI RTPENAESWL
RDRLQKHDRI MGFGHRVYRT EDPRSRVLKE LARQIVDPSL FELATTVEDT ARRLLREQHP
ERPIDVNVEF YSSVVLHAVG IPPELFTCTF ACARTVGWTA HIVEQLQDNR LFRPDAEYVG
PEGLTLEATP PGTSA
//
