ID A0A2P8VSQ7_9CYAN Unreviewed; 351 AA.
AC A0A2P8VSQ7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN ORFNames=C7271_25765 {ECO:0000313|EMBL:PSN10609.1};
OS filamentous cyanobacterium CCP5.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107701 {ECO:0000313|EMBL:PSN10609.1, ECO:0000313|Proteomes:UP000240885};
RN [1] {ECO:0000313|EMBL:PSN10609.1, ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|EMBL:PSN10609.1,
RC ECO:0000313|Proteomes:UP000240885};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|Proteomes:UP000240885};
RA Moore K., Momper L.;
RL Submitted (MAR-2018) 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}.
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:PSN10609.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PYEQ01000811; PSN10609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8VSQ7; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000240885; 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 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:UP000240885}.
FT DOMAIN 15..304
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 351 AA; 38421 MW; 3ED17D18EDF5BA2F CRC64;
MQTLNPPTTQ PRSQQFASDN YSGICPEALE YMLAANAGDV PAYGNDEWTQ RAADRFRDLF
ETDCEVFFTF NGTAANSLAL ASLCQSYHSV ICHELAHIET DECGAPEFAS NGSKLLLASG
DNGKLAPEAV EKIITKRSDI HYPKPKVISL TQTTEVGTLY SPAELLALRE LANHYSLRIH
MDGARFANAV VSSGLSPAEL TWQSGVDVLC FCGTKNGMAV GEAILFFDRP LAEDFAYRCK
QAGQLASKMR FISAPWLGLL ETGAWLRNAE HANRMAAYLE DQLRGLGLSL MFPRQANGVF
VEMPEPAIER MREKGWLFYT FIGVGGVRLM CAWNTTAAAI DALVADIKAA L
//
