ID A0A0Q5CY02_9BURK Unreviewed; 335 AA.
AC A0A0Q5CY02;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Aldolase {ECO:0000313|EMBL:KQQ31962.1};
GN ORFNames=ASF61_16625 {ECO:0000313|EMBL:KQQ31962.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ31962.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ31962.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ31962.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ31962.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ31962.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQQ31962.1}.
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DR EMBL; LMNW01000035; KQQ31962.1; -; Genomic_DNA.
DR RefSeq; WP_056160561.1; NZ_LMNW01000035.1.
DR AlphaFoldDB; A0A0Q5CY02; -.
DR STRING; 1736266.ASF61_16625; -.
DR OrthoDB; 8481499at2; -.
DR Proteomes; UP000051032; 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; 6.10.140.960; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR040186; Citramalyl-CoA_lyase.
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; PTHR11105:SF0; CITRAMALYL-COA LYASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11105; CITRATE LYASE SUBUNIT BETA-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|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 47..252
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 335 AA; 36011 MW; 76B1B6AFD4867446 CRC64;
MHPSEVLFQG NRQPLLLPAC DHYAGAEKLM RKSMSLQQEL GPVFDITLDC EDGASAGNEE
AHAHLVSALL ASGDNHYRRI GARVHDVHSP HFARDIATIA GGAGARALAY IVLPKVDSVA
EVAEAIAFIN GHAASAGRSD LPVHVLIETH GALRDAYAIA ALPQVQCLSF GIMDFVSAHY
GAIPGSAMRT PGQFTHPLVV RAKLEMAAAC HAHGKVSSHN VTTEIKDTAV AANDAQRAAA
EFGYTRMWSI HPDQIKPIVK AFTPRLSEVN EAAAILHEAA SVQWGPISQN GRLHDRASYR
YYWTILQRAR LAGLTLPESA AALMQPSPVH PLEPH
//
