ID A0A495WBY9_9PSEU Unreviewed; 428 AA.
AC A0A495WBY9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JUN-2023, entry version 10.
DE SubName: Full=2-methylisocitrate lyase-like PEP mutase family enzyme {ECO:0000313|EMBL:RKT57348.1};
GN ORFNames=C8E97_6067 {ECO:0000313|EMBL:RKT57348.1};
OS Saccharothrix australiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=2072 {ECO:0000313|EMBL:RKT57348.1, ECO:0000313|Proteomes:UP000282084};
RN [1] {ECO:0000313|EMBL:RKT57348.1, ECO:0000313|Proteomes:UP000282084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43800 {ECO:0000313|EMBL:RKT57348.1,
RC ECO:0000313|Proteomes:UP000282084};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKT57348.1}.
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DR EMBL; RBXO01000001; RKT57348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495WBY9; -.
DR Proteomes; UP000282084; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905:SF16; CARBOXYPHOSPHONOENOLPYRUVATE PHOSPHONOMUTASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_5G07230); 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:RKT57348.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282084}.
SQ SEQUENCE 428 AA; 44167 MW; 2F8035416302EF4E CRC64;
MNHDVLLDPT YTVPAVPHAT RGVAWLRAHV ARFSEGADHE RRRALAVSHL STVDLAALRR
PGNAVAKLAA GLGLPRAVVA DVSVVARCYQ PHTTATPEAD AAVARLVAAC GGAWDEATAA
RIGLLVQASA ATDAMVAGRV PPVPATRRVA PDGTVVEVSL ADAPFGAGRH ECPGRAHAAA
LAEGTFHRLH AGPEPLVLPN AWDHASAAAL VRAGFPAIGT TSLGVAAAAG LPDAAGVARA
ETLALARRLV RLPVPVTVDV EAGFGDVRGL AAELADLGVA GVNIEDGRGD GLADPAEQAD
LLRAFKDAAP HLFLNARVDT HWLRVDREST VERALRYVDA GADGVFVPGL AADRDIAEVV
EAVPVPVNVL AQRDVRALAA LGVRRISTGS LLFRAAVRAT VATARAVRDG EPVGEVPGYD
EVRALADL
//