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Database: UniProt
Entry: A0A1X2D8K9_9MYCO
LinkDB: A0A1X2D8K9_9MYCO
Original site: A0A1X2D8K9_9MYCO 
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
//
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