ID A0A1F2ZUJ7_9PROT Unreviewed; 304 AA.
AC A0A1F2ZUJ7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Host specificity protein {ECO:0000313|EMBL:OFW97652.1};
GN ORFNames=A3D94_18040 {ECO:0000313|EMBL:OFW97652.1};
OS Alphaproteobacteria bacterium RIFCSPHIGHO2_12_FULL_66_14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1797225 {ECO:0000313|EMBL:OFW97652.1, ECO:0000313|Proteomes:UP000176194};
RN [1] {ECO:0000313|EMBL:OFW97652.1, ECO:0000313|Proteomes:UP000176194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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:OFW97652.1}.
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DR EMBL; MEMN01000210; OFW97652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2ZUJ7; -.
DR STRING; 1797225.A3D94_18040; -.
DR Proteomes; UP000176194; 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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 16..234
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 304 AA; 32859 MW; 4BC731397867230D CRC64;
MTGRPLLSRP APPVWRSTLY VPGNVPKFID KAHERGADCV LVDLEDSVQP AQKSEARAML
PETMKKVARG GADVAVRINR PLRLAIPDIE AAVRPGLSAL FITKTEGVQH LRLLDEMVTE
LERERGMPVG GVGFGAMIEH PRALAQIHDI AEHGPRVIAM MLGGEDFALE TGSVPSDESL
ELPKRLVAFA AQAHGVAMMG ILGTVADYSD PAAYKKSAER ARRFGFSGGT CIHPGLVPAL
NEAFTPGADE VAYARKLIAA DQKAAAEGRG SFSVDGKMID IPVIDRARRL IERHEAIERR
LKRA
//
