ID F5YH96_TREPZ Unreviewed; 348 AA.
AC F5YH96;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=L-allo-threonine aldolase (L-allo-TA) (L-allo-threonineacetaldehyde-lyase) {ECO:0000313|EMBL:AEF84377.1};
DE EC=4.1.2.- {ECO:0000313|EMBL:AEF84377.1};
GN OrderedLocusNames=TREPR_1108 {ECO:0000313|EMBL:AEF84377.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84377.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF84377.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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; CP001843; AEF84377.1; -; Genomic_DNA.
DR RefSeq; WP_015708963.1; NC_015578.1.
DR AlphaFoldDB; F5YH96; -.
DR STRING; 545694.TREPR_1108; -.
DR KEGG; tpi:TREPR_1108; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_4_12; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000009223; Chromosome.
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; 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;
KW Lyase {ECO:0000313|EMBL:AEF84377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT DOMAIN 3..280
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 348 AA; 37577 MW; 1CD14DF146F6E5BD CRC64;
MIDIRSDTVT GPTEAMRKAM ANAEVGDDVY GDDPTVNRLE KMGAEILDKE ASLFVPSGTF
GNQLALFTWC PRGTEVILGE ECHIIQHEAG AASVIAGVQT RPISAPDGVL RPAALLERLR
KAELHYPATS LICLENAHSL GRAVPVEAMD EVRDLAGQWG LPVHLDGARL FNAAAALKRE
AREIAARADS VMFCLSKGLC APVGSLLAGK REFVEAARFK RKIMGGGMRQ AGILAAAGII
ALEDQAGRLR EDHGRARFLE KELAAIPGIT LSPGDINMVY FSFPPAEDPK IAGGITEFFL
KQNIRINGPE RGIFRFVTHH WIGDAEIKTI LEASQEAFGE QFSKKAAP
//
