ID A0A0S9Q123_9ACTN Unreviewed; 364 AA.
AC A0A0S9Q123;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aldolase {ECO:0000313|EMBL:KQP63468.1};
GN ORFNames=ASF47_15450 {ECO:0000313|EMBL:KQP63468.1};
OS Nocardioides sp. Leaf285.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP63468.1, ECO:0000313|Proteomes:UP000051495};
RN [1] {ECO:0000313|EMBL:KQP63468.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP63468.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP63468.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP63468.1,
RC ECO:0000313|Proteomes:UP000051495};
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:KQP63468.1}.
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DR EMBL; LMNH01000004; KQP63468.1; -; Genomic_DNA.
DR RefSeq; WP_056864901.1; NZ_LMNH01000004.1.
DR AlphaFoldDB; A0A0S9Q123; -.
DR Proteomes; UP000051495; 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:UP000051495}.
FT DOMAIN 30..199
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 364 AA; 39208 MW; 5EF763319E1115E7 CRC64;
MRPSKDFFRP LAVGAPTPPT DIPARPSRAI HFFDPSNAKM AAKIPQMVGG VDVLLGNLED
AVKADNKVAA REGLVRIGQE TEGLGGPDSP TQLWTRINSL DSPWALDDLT TLVPAIGHKL
DVVMVPKVQG AEDIHYVDRL LAQLEAKAGL DRPILVHAIL ETARGMANVE EICGASPRMQ
GLSLGPADLA ADRRMKTTRV GGGHPGYLVR QDPPRNELGV AEIEAPRSVF QQDLWHYTIA
RMVDACAMHG IYPYYGPFGD IADVVACEDQ FRNAFLLGCV GTWSLHPKQI AIAHRVFSPS
VEDVAHARRV VAAMGDGTGA VMLDGKMEDD ASLKQCLVMV ELAEQLAAID PELAEQYAAA
GSED
//
