ID   A0A075JHG8_9MICO        Unreviewed;       281 AA.
AC   A0A075JHG8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Aldolase {ECO:0000313|EMBL:AIF41611.1};
GN   ORFNames=HX89_12455 {ECO:0000313|EMBL:AIF41611.1};
OS   Dermacoccus nishinomiyaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF41611.1, ECO:0000313|Proteomes:UP000027986};
RN   [1] {ECO:0000313|EMBL:AIF41611.1, ECO:0000313|Proteomes:UP000027986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M25 {ECO:0000313|EMBL:AIF41611.1,
RC   ECO:0000313|Proteomes:UP000027986};
RA   Hong K.W., Chan K.G.;
RT   "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL   Submitted (JUL-2014) 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; CP008889; AIF41611.1; -; Genomic_DNA.
DR   RefSeq; WP_006943934.1; NZ_VECS01000002.1.
DR   AlphaFoldDB; A0A075JHG8; -.
DR   GeneID; 41841881; -.
DR   KEGG; dni:HX89_12455; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_2_0_11; -.
DR   OrthoDB; 4322898at2; -.
DR   Proteomes; UP000027986; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   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:UP000027986}.
FT   DOMAIN          19..217
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   281 AA;  29932 MW;  ADC666C504BC4F9E CRC64;
     MFSGRNARAA ALPAQLSRSW LLASAMKPEL FDAALASEAD SVIFDIEDAA PAADKSTARD
     NVVKALEDGA TGWVRINDIN TEFWEDDLNA LHGIPGLRGV MLAKTEKPEH VTLTAMRLNP
     GTPVLALVES AIGIENATSI ASAPGTFRLA FGVGDFRRDT GAGADPMALA YARSKLVVAS
     RVGQLPGPID GPTLTDSEDE LLEACKVTQN MGMTGKLTLR IDQTDPINRG LSPSHSEIEW
     AAELLDSHEH GGGTRDGSYA PRLARAQKIR NLGESYGLWT V
//