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Database: UniProt
Entry: I4BLV9_MYCCN
LinkDB: I4BLV9_MYCCN
Original site: I4BLV9_MYCCN 
ID   I4BLV9_MYCCN            Unreviewed;       271 AA.
AC   I4BLV9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Citrate lyase beta subunit {ECO:0000313|EMBL:AFM18266.1};
GN   OrderedLocusNames=Mycch_3530 {ECO:0000313|EMBL:AFM18266.1};
OS   Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM18266.1, ECO:0000313|Proteomes:UP000006057};
RN   [1] {ECO:0000313|EMBL:AFM18266.1, ECO:0000313|Proteomes:UP000006057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB4 {ECO:0000313|EMBL:AFM18266.1,
RC   ECO:0000313|Proteomes:UP000006057};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP003053; AFM18266.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4BLV9; -.
DR   STRING; 710421.Mycch_3530; -.
DR   KEGG; mcb:Mycch_3530; -.
DR   PATRIC; fig|710421.3.peg.3531; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_2_1_11; -.
DR   Proteomes; UP000006057; 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:AFM18266.1};
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:UP000006057}.
FT   DOMAIN          10..210
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   271 AA;  28930 MW;  2F974F79F4F847F0 CRC64;
     MLGNNGPGWL FCPADRPERF AKAAAAADVV ILDLEDGVAA KDREAARTAL IETPLDPART
     VVRVNPVGTP DHAADVEALA ATDYTTVMLA KTETAEQVAS LAPRHVVVLV ETPLGALAVT
     ETARVENAYA VMWGAEDLFA VTGGTNNRWP DGTYRDVARH VRSQSLLAAK AYGRLALDSV
     YLDIKDLDGL RAEGDDAVAV GFDAKVAIHP TQVAVIRAAY APTDEQVDWA RRVLDTAQTE
     RGVFAFEGIM VDAPVLRRAE RIVALAPHPG S
//
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