ID A0A1X2D8K9_9MYCO Unreviewed; 273 AA.
AC A0A1X2D8K9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:ORW84264.1};
GN ORFNames=AWC22_13555 {ECO:0000313|EMBL:ORW84264.1};
OS Mycobacterium riyadhense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=486698 {ECO:0000313|EMBL:ORW84264.1, ECO:0000313|Proteomes:UP000193087};
RN [1] {ECO:0000313|EMBL:ORW84264.1, ECO:0000313|Proteomes:UP000193087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45176 {ECO:0000313|EMBL:ORW84264.1,
RC ECO:0000313|Proteomes:UP000193087};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) 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:ORW84264.1}.
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DR EMBL; LQPQ01000037; ORW84264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2D8K9; -.
DR STRING; 486698.AWC22_13555; -.
DR OrthoDB; 5172636at2; -.
DR Proteomes; UP000193087; 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:ORW84264.1};
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 11..211
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 112
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"
SQ SEQUENCE 273 AA; 28997 MW; 9586FD04B4708763 CRC64;
MSLRDAGPGW LFCPADRPER FAKAAAAADV VILDLEDGVA VHEKPVARQA LQDTPLDPAH
TVVRINGAGT DEQARDLEAL AGTAYTTVML PKAESAEQVA ALAPRDVIAL VETARGALFA
AEIAAAENTV GMMWGAEDLI ATLGGSSSRR ADGAYRDVTR HVRSTILLVA SAFDRLALDA
VHLDISDIEG LQEEALDAAA VGFDVTVCIH PSQVAVVRKA YRPGDEKLAW ARRVLAASRN
ERGVFAFEGQ MVDSPVLRHA EMLLRRAGES APG
//