ID E1VX48_GLUAR Unreviewed; 353 AA.
AC E1VX48;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:CBT76201.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:CBT76201.1};
GN OrderedLocusNames=AARI_19820 {ECO:0000313|EMBL:CBT76201.1};
OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN [1] {ECO:0000313|EMBL:CBT76201.1, ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RX PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA Vallaeys T.;
RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT adaptation to the surface of cheese.";
RL PLoS ONE 5:E15489-E15489(2010).
RN [2] {ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RA Genoscope.;
RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT CIP 108037 / JCM 13566 / Re117).";
RL Submitted (JUL-2010) 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}.
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DR EMBL; FQ311875; CBT76201.1; -; Genomic_DNA.
DR RefSeq; WP_013349325.1; NC_014550.1.
DR AlphaFoldDB; E1VX48; -.
DR STRING; 861360.AARI_19820; -.
DR KEGG; aai:AARI_19820; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_049619_0_0_11; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000006878; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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:CBT76201.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006878}.
FT DOMAIN 12..298
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 353 AA; 38423 MW; 5F46D4C9F3D8B8C6 CRC64;
MTSPHDISVR GFASDNYSGV HPRVMDAIAR ANGGHQIAYG EDHYTEELGN VARNVFGPEA
QIFPVFNGTG ANVTALQSLL PRWGAVICAS SAHINVDENG APERVGGFKL LQVDTPDGKL
TPELIDKEAW GWGDEHRAQP LAVSITQATE LGTIYTPEEI KAITDHAHKL GMNVHLDGSR
LSNAAASLNV PLRALTTDAG VDIVSLGGTK NGILLGEGIL TLRSELAADL KYLRKMNMQL
SSKMRFISAQ LIELYGTELW RELASHSNAM AAKLSQAVGD IEGVELVYPT QANGVFAQLP
TEISDQLREH FRFYDWDRAA GQVRWMCSFD TTEEDVEAFI SKLRELCGAY ATA
//
