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Database: UniProt
Entry: A0A3S9Q3C6_9GAMM
LinkDB: A0A3S9Q3C6_9GAMM
Original site: A0A3S9Q3C6_9GAMM 
ID   A0A3S9Q3C6_9GAMM        Unreviewed;       339 AA.
AC   A0A3S9Q3C6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:AZQ83356.1};
DE            EC=4.1.2.48 {ECO:0000313|EMBL:AZQ83356.1};
GN   ORFNames=EKO29_04375 {ECO:0000313|EMBL:AZQ83356.1};
OS   Colwellia sp. Arc7-635.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=2497879 {ECO:0000313|EMBL:AZQ83356.1, ECO:0000313|Proteomes:UP000286937};
RN   [1] {ECO:0000313|EMBL:AZQ83356.1, ECO:0000313|Proteomes:UP000286937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arc7-635 {ECO:0000313|EMBL:AZQ83356.1,
RC   ECO:0000313|Proteomes:UP000286937};
RA   Lin J.;
RT   "Complete Genome Sequences of Colwellia sp. Arc7-635, a Denitrifying
RT   Bacterium Isolated from Arctic Seawater.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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DR   EMBL; CP034660; AZQ83356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9Q3C6; -.
DR   KEGG; cov:EKO29_04375; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000286937; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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:AZQ83356.1}.
FT   DOMAIN          3..283
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   339 AA;  36375 MW;  82146A8B58D952A6 CRC64;
     MIDFRSDTVT RPSKAMRTAM ANAEVGDDVY GDDPTVNELE SWAAKRHGFA SAMFCSSGTQ
     ANLLALMAHC QRGDEYLCGQ QAHNYKFEGG GAAILGSIQP QPIANEPDGT LCFKKLAAAI
     KPDDSHFART TLLSIENTIN GKVLPLSYMA EAREFTSQNN LALHLDGARV YNAASALNVD
     ITEICQHVDS MSICLSKGLG APIGSLLLGS EALIKSAKRW RKVVGGGMRQ AGIIAAAAKI
     ALEENSVKLQ QDHSNAKYLA HALNELEGIS VNLAHVETNM LFATLAEDIN VADLVEELKS
     KDVLLTAGNP MRLVTHLDID KADIDQFITL LTIALNKAG
//
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