ID A0A3B0BET9_9BACL Unreviewed; 278 AA.
AC A0A3B0BET9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Aldolase {ECO:0000313|EMBL:RKN70607.1};
GN ORFNames=D7M11_30530 {ECO:0000313|EMBL:RKN70607.1};
OS Paenibacillus ginsengarvi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN70607.1, ECO:0000313|Proteomes:UP000282311};
RN [1] {ECO:0000313|EMBL:RKN70607.1, ECO:0000313|Proteomes:UP000282311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN70607.1,
RC ECO:0000313|Proteomes:UP000282311};
RX PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA Yoon M.H., Ten L.N., Im W.T.;
RT "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT cultivation.";
RL Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
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:RKN70607.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RBAH01000031; RKN70607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0BET9; -.
DR OrthoDB; 86160at2; -.
DR Proteomes; UP000282311; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000282311}.
FT DOMAIN 31..245
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
SQ SEQUENCE 278 AA; 30592 MW; BC4EFF7FADB02EDC CRC64;
MPEKYTMRPS RVLEKLRKGE VAYATKLNLG DARAAEIAAM SGFDCIWTDM EHVPNDWSAV
EKQILAAKAH GVDTVVRVAR GSYSDLVRPL EMDATAVMVP HIMSLSDAKS VVRCTKFYPL
GMRPVDGGNA DGAYCNIELA DYLQQANAER FNILQIEDVE PLDELEDIIA LPGLDMIFFG
PGDFSQSIGA PGQMDHPLIG ETRKRIAELA AKHGKFAGTV GSTASSEELI AMGYRFISVG
ADVVALSQYF RNIVRELHKQ EEIRVNGVYA DRKEKVSP
//
