ID A0A161HBQ2_9RHOB Unreviewed; 350 AA.
AC A0A161HBQ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN ORFNames=AKL17_0940 {ECO:0000313|EMBL:AMY68199.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY68199.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY68199.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012661; AMY68199.1; -; Genomic_DNA.
DR RefSeq; WP_066810122.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A161HBQ2; -.
DR STRING; 1335048.AKL17_0940; -.
DR KEGG; daa:AKL17_0940; -.
DR PATRIC; fig|1335048.3.peg.976; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000076128; Chromosome.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA.
DR GO; GO:0006567; P:threonine catabolic process; IEA:UniProtKB-UniRule.
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}.
FT DOMAIN 3..292
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 350 AA; 37118 MW; 0BC32F1EE7ABF953 CRC64;
MNFASDNTSA AAPEVMAALQ AANTGYAAPY GNDPIMDRVR AKLREIFEAP EAAVYLVATG
TAANALSLAI LTQPWGAVFC HRNAHVEEDE CGAPEFYTNG AKLVLVEGAH AKMTPEGLHK
AINFIGRGGI HNVQRGMVTI TNATENGTVF FPSEVKALAD VARGFGLPVH MDGARFANAI
VATGATPAEM TWKAGVDVLS FGGTKNGCMG VEAVVIFDPA RAREFELRRK RGGHLFSKHR
FLSAQMEAYL TDGLWLRLAG QANAAAARLS SALLAAPQTS LVHPCEANAV FAAFPRAGHR
RAQAAGAAYY LWPGDQSMEG PDDEALAARL VCSWSTTDAD VDDFVALIRG
//
