ID F3PPY0_9BACE Unreviewed; 457 AA.
AC F3PPY0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Beta-eliminating lyase {ECO:0000313|EMBL:EGF59022.1};
GN ORFNames=HMPREF9446_00772 {ECO:0000313|EMBL:EGF59022.1};
OS Bacteroides fluxus YIT 12057.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF59022.1, ECO:0000313|Proteomes:UP000003416};
RN [1] {ECO:0000313|EMBL:EGF59022.1, ECO:0000313|Proteomes:UP000003416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF59022.1,
RC ECO:0000313|Proteomes:UP000003416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR611166-50};
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000256|ARBA:ARBA00009721}.
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:EGF59022.1}.
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DR EMBL; AFBN01000013; EGF59022.1; -; Genomic_DNA.
DR RefSeq; WP_009124029.1; NZ_GL882614.1.
DR AlphaFoldDB; F3PPY0; -.
DR STRING; 763034.HMPREF9446_00772; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_10; -.
DR Proteomes; UP000003416; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR CDD; cd00617; Tnase_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR011166; Beta-eliminating_lyase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR32325; BETA-ELIMINATING LYASE-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32325:SF4; TRYPTOPHANASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF001386; Trpase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EGF59022.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR611166-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000003416}.
FT DOMAIN 47..422
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 257
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 457 AA; 51870 MW; D8E776D10F27DEB0 CRC64;
MELPFAESWK IKMVEPIRKS TRQEREQWLK EAHYNVFQLK SEQVYIDLIT DSGTGAMSDR
QWAGMMLGDE SYAGASSFFK LKETITRLTG FEYVIPTHQG RAAENVLFSY LVHEGDIVPG
NSHFDTTKGH IEGRKAIALD CTIDEAKQTQ LEIPFKGNVD PAKLEKALQE HSNHIPFIIV
TVTNNTAGGQ PVSMQNLREV RAIADKYHKP VLFDSARFAE NAYFIKTREN GYSDKSIKEI
TREMFALADG MTMSAKKDGI VNMGGFIATR KKDWYEGAKG FCVQFEGYLT YGGMNGRDMN
ALAIGLDENT EFDNLETRIR QVEYLAKKLD EYGIPYQRPA GGHAIFVDAP KVLTRVPKEE
FPAQTLTVEL YLEAGIRGCE IGYLLADRDP VTRENRFNGL DLLRLAIPRR VYTDNHMNVI
AAALKNVYDK RESITRGVRI AWEAPLMRHF TVQLERL
//
