ID A9CFN2_AGRFC Unreviewed; 350 AA.
AC A9CFN2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN Name=ald {ECO:0000313|EMBL:AAK89623.1};
GN OrderedLocusNames=Atu3785 {ECO:0000313|EMBL:AAK89623.1};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK89623.1, ECO:0000313|Proteomes:UP000000813};
RN [1] {ECO:0000313|EMBL:AAK89623.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2] {ECO:0000313|EMBL:AAK89623.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
CC -!- FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to
CC glycine and acetaldehyde. {ECO:0000256|PIRNR:PIRNR038940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-allo-threonine = acetaldehyde + glycine;
CC Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:58585; EC=4.1.2.48;
CC Evidence={ECO:0000256|PIRNR:PIRNR038940};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48;
CC Evidence={ECO:0000256|PIRNR:PIRNR038940};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR038940};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966, ECO:0000256|PIRNR:PIRNR038940}.
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DR EMBL; AE007870; AAK89623.1; -; Genomic_DNA.
DR PIR; AE3022; AE3022.
DR PIR; E98262; E98262.
DR RefSeq; NP_356838.1; NC_003063.2.
DR RefSeq; WP_006313436.1; NC_003063.2.
DR AlphaFoldDB; A9CFN2; -.
DR SMR; A9CFN2; -.
DR STRING; 176299.Atu3785; -.
DR EnsemblBacteria; AAK89623; AAK89623; Atu3785.
DR GeneID; 66224073; -.
DR KEGG; atu:Atu3785; -.
DR PATRIC; fig|176299.10.peg.3623; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_049619_0_0_5; -.
DR OrthoDB; 9774495at2; -.
DR PhylomeDB; A9CFN2; -.
DR BioCyc; AGRO:ATU3785-MONOMER; -.
DR Proteomes; UP000000813; Chromosome linear.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA.
DR GO; GO:0006567; P:threonine catabolic process; IEA:UniProtKB-UniRule.
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; IPR026273; Low_specificity_L-TA_bact.
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 PIRSF; PIRSF038940; Low_specificity_LTA; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|PIRNR:PIRNR038940};
KW Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR038940};
KW Reference proteome {ECO:0000313|Proteomes:UP000000813}.
FT DOMAIN 3..291
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 350 AA; 38110 MW; 64168506A1C99B53 CRC64;
MFFASDNWAG AHPAVNERLS RESTRFAAAY GTSELDLSIE KRFNEIFERE VAVFFVATGT
AANSLSLASI ARPGGLTFCH SEAHVIEDEC GAPDFFSGMR MVAVEGPDGK MLPENLIERI
ARYPQDAVHH GRAAAITMTQ ATEAGTVYTL DEIDAISKIA KENGLPLHMD GARFANALAA
LGTTPAEMTW KRGVDVLSFG GTKNGCWCAE AIVFFDPSLA RDFSFLRKRT AQLFSKSRFI
AAQFEAYLQD DLWLGLAGHA NAMANRLRAG FGSLNSARLA WPTQANEVFA ILPKAAAEAA
TQKGAKFYDW LEPRDMPENV GKDEVLIRMV TSFATTEADV DEFLSICAAV
//
