ID H0BZ86_9BURK Unreviewed; 279 AA.
AC H0BZ86;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:EHL22260.1};
GN ORFNames=KYG_13581 {ECO:0000313|EMBL:EHL22260.1};
OS Acidovorax sp. NO-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL22260.1, ECO:0000313|Proteomes:UP000003485};
RN [1] {ECO:0000313|EMBL:EHL22260.1, ECO:0000313|Proteomes:UP000003485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NO-1 {ECO:0000313|EMBL:EHL22260.1,
RC ECO:0000313|Proteomes:UP000003485};
RX PubMed=22374962; DOI=10.1128/JB.06814-11;
RA Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL J. Bacteriol. 194:1635-1636(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AGTS01000083; EHL22260.1; -; Genomic_DNA.
DR RefSeq; WP_008905390.1; NZ_AGTS01000083.1.
DR AlphaFoldDB; H0BZ86; -.
DR STRING; 512030.KYG_13581; -.
DR PATRIC; fig|512030.4.peg.2672; -.
DR OrthoDB; 348111at2; -.
DR Proteomes; UP000003485; Unassembled WGS sequence.
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:UP000003485}.
FT DOMAIN 15..218
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 279 AA; 29563 MW; 0CD9F629D9C1BA7E CRC64;
MTAHTSGPKA LLHAYLFVPA DRPERIAKAR ASGADAVIVD LEDAVAPEAK VRAREALAAL
LDEAAPLVVR INAAGTPWFD DDLELCRHPG VAAIMLPKAE GIDAVCTVVE TTYQDVLPII
ESARGLHEMD SIARVPGVIR LAFGSVDLAL DLGIECAPDG TEIELLAFRS QLVLASRLAG
LAAPVDGVST AIDDLQRLQA DTERSRRLGF GAKLCIHPKQ LATVQAVFTP SPERLDWARR
VCKAFETAGG SAVAVDGQMV DLPVVQRARA VLRDAGLSA
//