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Database: UniProt
Entry: A0A261SI80_9BORD
LinkDB: A0A261SI80_9BORD
Original site: A0A261SI80_9BORD 
ID   A0A261SI80_9BORD        Unreviewed;       351 AA.
AC   A0A261SI80;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OZI36053.1};
GN   ORFNames=CEG14_13535 {ECO:0000313|EMBL:OZI36053.1};
OS   Bordetella genomosp. 1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395607 {ECO:0000313|EMBL:OZI36053.1, ECO:0000313|Proteomes:UP000217005};
RN   [1] {ECO:0000313|EMBL:OZI36053.1, ECO:0000313|Proteomes:UP000217005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17610 {ECO:0000313|EMBL:OZI36053.1,
RC   ECO:0000313|Proteomes:UP000217005};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) 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:OZI36053.1}.
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DR   EMBL; NEVL01000003; OZI36053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SI80; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000217005; 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; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          13..293
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   351 AA;  36847 MW;  A766D5E6BA8B266C CRC64;
     MSSPSELPRH PVDLRSDTVT RPTPAMYERM MHAPIGDDGL DGDPSVHALE AEVATRLGKD
     AGLFVPSCTM ANLLAVLAQT QRNEQVVLEG TAHMYTSERG AATFTNLFYL GVTGVDGAMD
     LDRLADALQA GGHKLKTSLV AMETTHNNAG GTVLPLAHMA AVHALARDRG AAVHLDGARL
     FNAAVALGVA PAEITQHTDT VSLCLSKGLS APVGAVLAGP RKQIDVARTL RRMLGGTQRQ
     SGIMAAAALE GVQHMGARLA EDHTRARRLS DGINALGGPI TATVPQTNIV QVEVGATAMS
     NKEWVAALEA AGLKIRPWAN TRLRCVTHRH TTDADITAAL AAFSQVLAAP R
//
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