ID A0A0D6DWZ0_9LACT Unreviewed; 512 AA.
AC A0A0D6DWZ0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 Name=citF {ECO:0000313|EMBL:CEN28279.1};
GN ORFNames=LACPI_1079 {ECO:0000313|EMBL:CEN28279.1};
OS Lactococcus piscium MKFS47.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN28279.1, ECO:0000313|Proteomes:UP000033166};
RN [1] {ECO:0000313|Proteomes:UP000033166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA Andreevskaya M.;
RL Submitted (JAN-2015) 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}.
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DR EMBL; LN774769; CEN28279.1; -; Genomic_DNA.
DR RefSeq; WP_047915440.1; NZ_LN774769.1.
DR AlphaFoldDB; A0A0D6DWZ0; -.
DR STRING; 1364.LP2241_30066; -.
DR KEGG; lpk:LACPI_1079; -.
DR HOGENOM; CLU_046521_2_0_9; -.
DR Proteomes; UP000033166; Chromosome I.
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:CEN28279.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR009451}.
SQ SEQUENCE 512 AA; 55097 MW; 657CC903A75DA0F7 CRC64;
MKNKVNRELP DEITKRYEYM PFTTSNYGGV ITQRSGPKVR ATTGKEKCAY TLEEVIVKTV
QDGMTLSFHH HFREGDYVFN AVMRLIIDLG YKNLALAPSS LTNVMNDIVV EAIEKGVVTQ
ITSSGMRGKL GEAVSHGALQ TPIVLRSHGG RARAIETGDI KIDVAFLGVP NSDEMGNANG
MVGASACGAL GYALMDAQYA QTVVLVTDHF VPYPNMPASI KQTQVDYVVE IAAVGDPDKI
GSGATRFTSD PKELKIAKTV NQVLTNSPYF KDGFSFQTGT GGAALAVSRF LRQSMIDQHI
KASFALGGIT SAMVDLLKEG LVGKLMDVQD FDRGAAQSMH ENENQQEIDA SWYADPANKG
AMVDQLDIVI LSALEIDTAF NVNVMTGSDG VIRGAIGGHQ DAATANLTII AAPLVRGRLA
TIVPRVTTVI TPGDTIDVVV TEVGIAINPR RSDLLDSLTQ IPDFPIFTIQ ELQAKAAAKT
GIPEPLTFTD KVVAFVEYRD GTLIDVINQI KE
//
