ID A0A1V2M0U2_9FIRM Unreviewed; 517 AA.
AC A0A1V2M0U2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Citrate lyase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE Short=Citrase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE EC=2.8.3.10 {ECO:0000256|PIRNR:PIRNR009451};
DE EC=4.1.3.6 {ECO:0000256|PIRNR:PIRNR009451};
DE AltName: Full=Citrate (pro-3S)-lyase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE AltName: Full=Citrate CoA-transferase subunit {ECO:0000256|PIRNR:PIRNR009451};
GN ORFNames=AN396_00750 {ECO:0000313|EMBL:ONI40868.1};
OS Epulopiscium sp. SCG-B11WGA-EpuloA1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1710701 {ECO:0000313|EMBL:ONI40868.1, ECO:0000313|Proteomes:UP000188605};
RN [1] {ECO:0000313|EMBL:ONI40868.1, ECO:0000313|Proteomes:UP000188605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCG-B11WGA-EpuloA1 {ECO:0000313|EMBL:ONI40868.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + citrate = (3S)-citryl-CoA + acetate;
CC Xref=Rhea:RHEA:19405, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57321; EC=2.8.3.10;
CC Evidence={ECO:0000256|PIRNR:PIRNR009451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089; EC=4.1.3.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR009451};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR009451}.
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:ONI40868.1}.
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DR EMBL; LJDB01000044; ONI40868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2M0U2; -.
DR STRING; 1710701.AN396_00750; -.
DR Proteomes; UP000188605; Unassembled WGS sequence.
DR GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008814; F:citrate CoA-transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2.
DR InterPro; IPR006472; Citrate_lyase_asu.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR01584; citF; 1.
DR PANTHER; PTHR40596; CITRATE LYASE ALPHA CHAIN; 1.
DR PANTHER; PTHR40596:SF1; CITRATE LYASE ALPHA CHAIN; 1.
DR Pfam; PF04223; CitF; 1.
DR PIRSF; PIRSF009451; Citrt_lyas_alpha; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR009451};
KW Lyase {ECO:0000256|PIRNR:PIRNR009451, ECO:0000313|EMBL:ONI40868.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR009451}.
SQ SEQUENCE 517 AA; 55690 MW; 20D019D3A939847E CRC64;
MKNVLGREVP DFVPGYGKVT PFKGAFKNFP EEGKRKAAPL IKYAIPRYGN KVVNNLEEVF
LKIGIKDGMT LSFHHHFRNG DKILTQVIDV AAKLGLKNLT VAASGIMLSH HGLVPHLKSG
VVTHIDTNGL MGAVAEYIAK GKMENPIVIR SHGGRARAIE AGDLHIYVAF MGASCADIYG
NMNGCEGNSI FGSIGYGILD SQYADYVVAV TDMVQEIPLS FISIPQTRVD YVVKLDTIGD
SKGIATGTLS LTKDPIQLDI ARNALKIVDA LGFIKDGFSF QTGGGGPSIA FTKFLKDLVK
ERNIKAGFAM GGITATIVEM LEEGLLSHAY DTQSFDLYSA KSIRKNQNHI EVGCDFYASP
FNNGCAVNGL DVCLIGAFEV DLDFNINCLT GMDGIARTGI GGNPDTAAGS KVSIVTANLI
RSRVPTIVEK VHTLCTPGES VDVIVTDRGI AVNPLRQDLI STLTQKGIKL NTIEELKEIA
ENIVGVPEEI KTTDKVVAVI EYRDGTILDT IRQVKEN
//
