ID U5RV89_9CLOT Unreviewed; 300 AA.
AC U5RV89;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Citrate lyase subunit beta {ECO:0000256|ARBA:ARBA00015712};
DE EC=4.1.3.34 {ECO:0000256|ARBA:ARBA00012258};
DE EC=4.1.3.6 {ECO:0000256|ARBA:ARBA00012914};
DE AltName: Full=Citrate (pro-3S)-lyase subunit beta {ECO:0000256|ARBA:ARBA00030255};
DE AltName: Full=Citryl-CoA lyase subunit {ECO:0000256|ARBA:ARBA00032495};
GN Name=citE {ECO:0000313|EMBL:AGY75278.1};
GN ORFNames=CAETHG_0602 {ECO:0000313|EMBL:AGY74831.1}, CAETHG_1053
GN {ECO:0000313|EMBL:AGY75278.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY75278.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY75278.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY75278.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
RN [2] {ECO:0000313|EMBL:AGY75278.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY75278.1};
RA Brown S., Nagaraju S.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Represents a citryl-ACP lyase.
CC {ECO:0000256|ARBA:ARBA00003671}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-citryl-CoA = acetyl-CoA + oxaloacetate;
CC Xref=Rhea:RHEA:20812, ChEBI:CHEBI:16452, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57321; EC=4.1.3.34;
CC Evidence={ECO:0000256|ARBA:ARBA00001238};
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|ARBA:ARBA00000263};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,gamma)6.
CC {ECO:0000256|ARBA:ARBA00011382}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC beta subunit subfamily. {ECO:0000256|ARBA:ARBA00005549}.
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DR EMBL; CP006763; AGY74831.1; -; Genomic_DNA.
DR EMBL; CP006763; AGY75278.1; -; Genomic_DNA.
DR RefSeq; WP_013239686.1; NZ_CP012395.1.
DR AlphaFoldDB; U5RV89; -.
DR KEGG; cah:CAETHG_0602; -.
DR KEGG; cah:CAETHG_1053; -.
DR PATRIC; fig|1341692.11.peg.1045; -.
DR HOGENOM; CLU_044864_0_0_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR006475; Citrate_lyase_beta_bac.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01588; citE; 1.
DR PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lyase {ECO:0000313|EMBL:AGY75278.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 6..225
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 300 AA; 32770 MW; 9DA0782941F94B08 CRC64;
MYKLRRTMMY VPGNNPGMVK DAHIYGADSL MFDLEDSVSL NEKDTARFLV YNALKSIDYE
GTETVVRING LDTPFGMEDL EAIVRAQPDV IRLPKTECAQ DVIDVEKEIE RIEKQSGIPV
GKTKIMAAVE SAIGVMNAYE IATASKRLMG IAIGAEDYVT NLKTTRSLDG IELLAGRSHV
LLAARAAGIY AFDTVFSDVN NEEGFINEVK LIKQLGFDGK SVINPRQIAP VHKIYTPSQK
EIDKSVRVIR AAKDAAEKGS GVVSLNGKMV DKPIIERAQR ALMLAEASGI CVSEGGEDID
//
