ID R5B405_9FIRM Unreviewed; 348 AA.
AC R5B405;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:CCX46211.1};
GN ORFNames=BN455_01491 {ECO:0000313|EMBL:CCX46211.1};
OS Firmicutes bacterium CAG:103.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1262999 {ECO:0000313|EMBL:CCX46211.1, ECO:0000313|Proteomes:UP000018290};
RN [1] {ECO:0000313|EMBL:CCX46211.1, ECO:0000313|Proteomes:UP000018290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:103 {ECO:0000313|Proteomes:UP000018290};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX46211.1}.
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DR EMBL; CAWL010000137; CCX46211.1; -; Genomic_DNA.
DR AlphaFoldDB; R5B405; -.
DR Proteomes; UP000018290; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000018290}.
FT DOMAIN 31..295
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 348 AA; 37167 MW; DD87BEF4BF5742D5 CRC64;
MLRFQNDYSE GAHPNVLRAL CDTNLCSTPG YGLDDDCRRA ADAIRARFAC PDADVHFLVG
GTQTNQLAAA AFLRPWEAMV AADTGHINVH ETGAIEATGH KVIAVPGADG KLTPAAIADA
AAQHCAAPGV YDEHMVLPRM VYVSDATELG TVYTRAELTA LRAACDAHGM YLYLDGARLA
QALTAAGSDL QPEDLPRLCD AFYIGGTKNG LLFGEAMVIV NDALKPGFRR AMKRNGAMLA
KGRLLGVQFA AAMEHDLWLE LGRHADAQAQ RIAAALSDRG IAMYVPSPTN QIFPILSDAQ
IARLQEQVAF NTTARVDAAH QAVRFVTSWA TTDAQVDALL AVLAQVLD
//