ID A0A0M8X092_9ACTN Unreviewed; 320 AA.
AC A0A0M8X092;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:KOV96411.1};
GN ORFNames=ADL04_17690 {ECO:0000313|EMBL:KOV96411.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV96411.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOV96411.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV96411.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KOV96411.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGDZ01000183; KOV96411.1; -; Genomic_DNA.
DR RefSeq; WP_030346773.1; NZ_LGDZ01000183.1.
DR AlphaFoldDB; A0A0M8X092; -.
DR PATRIC; fig|1519493.3.peg.3772; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000037702; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
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 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KOV96411.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037702}.
FT DOMAIN 11..241
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 320 AA; 35061 MW; FCC4EAFE0D377CEE CRC64;
MTTVNRLRPR RSCLAVPGSN PRFLEKAQGL PADQVFLDLE DACAPLAKPE ARHTIVKFLN
EGDWTGKTRV VRVNDWTTEW TYRDVVTVVE GAGQNLDCIM LPKVQSAEQV VALDLLLTQI
EKTMGFEVGR IGIEAQIENA QGLNNVNAIA QASPRLETII FGPADFMASI NMKSLVVGEQ
PPGYPADAYH YILMKILMAA RANDLQAIDG PYLQIRNVDG YREVAQRAAA LGFDGKWVLH
PGQVEASNEI FSPSQEDYDH AELILDAYDY YTSEAGGKKG SAMLGDEMID EASRKMALVI
AGKGRAAGMT RTSAFEIPEA
//
