ID   B3CIM6_9BACE            Unreviewed;       343 AA.
AC   B3CIM6;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Beta-eliminating lyase {ECO:0000313|EMBL:EDV04083.1};
GN   ORFNames=BACINT_03210 {ECO:0000313|EMBL:EDV04083.1};
OS   Bacteroides intestinalis DSM 17393.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV04083.1, ECO:0000313|Proteomes:UP000004596};
RN   [1] {ECO:0000313|EMBL:EDV04083.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV04083.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDV04083.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV04083.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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:EDV04083.1}.
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DR   EMBL; ABJL02000008; EDV04083.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3CIM6; -.
DR   STRING; 471870.BACINT_03210; -.
DR   eggNOG; COG2008; Bacteria.
DR   Proteomes; UP000004596; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EDV04083.1}.
FT   DOMAIN          8..285
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   343 AA;  38395 MW;  5E90BF97DFBA0CAE CRC64;
     MNITMRSFAS DNNSGVHPLV MEALNRANQN HAVGYGDDPW TEEAVRKIKE TFTADCEPLF
     VFNGTGSNAV ALQLATRPYN LILCAETAHI YVDECGAPAR MTGCQIRPIV TPDGKLTPEL
     VQPYLKNFGE QHHSQPGAIY ISQCSELGTV YTPEELKALT ALAHKHGMYV HMDGARLANA
     CVALNLSFKE LTVDCGIDIL SFGGTKNGLM LGESVVIFNP ELKKEALYVR KQSAQLASKL
     RYLSCQFTAY LTDDLWKKNA MHANAMAQKL YDGLKVFPGV HFTQKMESNQ LFLTMPRSVI
     DKLMKSYFFY FWNEAENEIR FVTSFDTTEE DIQTLLQAVK DSF
//