ID V4QRB3_9CAUL Unreviewed; 338 AA.
AC V4QRB3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN ORFNames=AEAC466_20705 {ECO:0000313|EMBL:ESQ81718.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ81718.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ81718.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ81718.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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}.
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:ESQ81718.1}.
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DR EMBL; AWGE01000026; ESQ81718.1; -; Genomic_DNA.
DR RefSeq; WP_023460116.1; NZ_AWGE01000026.1.
DR AlphaFoldDB; V4QRB3; -.
DR STRING; 1282362.AEAC466_20705; -.
DR PATRIC; fig|1282362.3.peg.4082; -.
DR eggNOG; COG2008; Bacteria.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000017826; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017826}.
FT DOMAIN 4..291
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 338 AA; 36133 MW; E6F0862F8222EC63 CRC64;
MANFASDNTA PVHPKVLQAL NDVNAGNAPA YGNDVVTEQL QQTFRTVFKA PDARVFPVFN
GSACNGLALA RMIRPYESIL CHQQAHINND ECGLPEFFTG GKIVGLSGDH AKLSVASIGS
LVEQTLEHAP HTSRPRVISL TQSTELGTVY SLSELADLSA FARAHGLYIH MDGARIANAV
ASLNCDPAKV VAGVDILSFG GTKNGAMLAE AAVILNPALA EDFAYVHKRA GQLPSKARYV
SAQLQALLDD DLWITLGRHA NAMAMALRDG LIDRAGVGLL HPVEANELFV TLPKVTADRL
FARGHRFYPW PNAGADAYRL VTSFATTDDE VAAFLADC
//
