ID A0A1Q7MF09_9CREN Unreviewed; 377 AA.
AC A0A1Q7MF09;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AUI93_05065 {ECO:0000313|EMBL:OLD11260.1};
OS Crenarchaeota archaeon 13_1_40CM_3_52_10.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805095 {ECO:0000313|EMBL:OLD11260.1, ECO:0000313|Proteomes:UP000186650};
RN [1] {ECO:0000313|EMBL:OLD11260.1, ECO:0000313|Proteomes:UP000186650}
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 ECO:0000256|PIRNR:PIRNR001369};
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: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:OLD11260.1}.
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DR EMBL; MNGO01000053; OLD11260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7MF09; -.
DR STRING; 1805095.AUI93_05065; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000186650; 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 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 262
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 313
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 377 AA; 42161 MW; 2AE4CD1F9ECBD5FA CRC64;
MTATTEIEKG LEGVVIAKSS ITFIDGERGI LRYRGIDINE LAAKSNFEEV TYLLWNGNLP
NKTQFSEFKK ELAAHRPLPT EVLKLLRATP KGAIPMEVAR TAVSYMATYP RKRGETFDQF
NRRKSLQLTA ALPTIVASYE RIRKGKTPIR PDPRLGHAAN FLYGLWGKKP DEAYRAAFDT
LSVLYADHEM NASTFAAIVA TSTLADLGGA VTSAIATLAG PLHGGSNQRV MEMLEEIGTL
DKVEGYIDSE LGAGRRIMGF GHRIYKTYDP RARILKTIAE KLTEERGNRK WLEIAEEVER
VVMDKRKLWP NIEFYAAVVL NALGVPKDLM PAVFACNRVS GWIAHIYEQY ADNRLIRPLT
EYVGPAQVPY VPIDQRA
//
