ID   V5XG49_MYCNE            Unreviewed;       270 AA.
AC   V5XG49;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:AHC26646.1};
GN   ORFNames=D174_19715 {ECO:0000313|EMBL:AHC26646.1};
OS   Mycolicibacterium neoaurum VKM Ac-1815D.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC26646.1, ECO:0000313|Proteomes:UP000018763};
RN   [1] {ECO:0000313|EMBL:AHC26646.1, ECO:0000313|Proteomes:UP000018763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC26646.1,
RC   ECO:0000313|Proteomes:UP000018763};
RX   PubMed=24435872;
RA   Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA   Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT   Strain VKM Ac-1815D.";
RL   Genome Announc. 2:e01177-13(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP006936; AHC26646.1; -; Genomic_DNA.
DR   RefSeq; WP_019511638.1; NC_023036.2.
DR   AlphaFoldDB; V5XG49; -.
DR   KEGG; mne:D174_19715; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_2_1_11; -.
DR   Proteomes; UP000018763; Chromosome.
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:AHC26646.1};
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:UP000018763}.
FT   DOMAIN          11..209
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   270 AA;  28623 MW;  8283EC94DD3B7390 CRC64;
     MSFANNGPAW IFCPADRPER FAKAAAAADV VILDLEDGAG DKPAARDAIV GTPLDPARTV
     IRINPHGTED QRLDLQALGR TGYTTVMLPK CEAPEQVMAL APLQVVLIVE TPLGALTVTE
     TAAAANTIGV MWGAEDLFGA LGGTTNRVAD GSYRDVAKHV RSQSLLAAKA HGKLALDSVY
     IDIKDLDGLR RETDDAVAVG FDIKVALHPT QVSVIRDGYA PTGEQVQWAR HVLAAAANHR
     GAFAFEGIMV DAPVLRRAER IVQLAPHPGS
//