ID I4EZV6_9ACTN Unreviewed; 348 AA.
AC I4EZV6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=L-allo-threonine aldolase {ECO:0000313|EMBL:CCH88919.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:CCH88919.1};
GN Name=ltaA {ECO:0000313|EMBL:CCH88919.1};
GN OrderedLocusNames=MODMU_3507 {ECO:0000313|EMBL:CCH88919.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88919.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88919.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88919.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; FO203431; CCH88919.1; -; Genomic_DNA.
DR RefSeq; WP_014741503.1; NC_017955.1.
DR AlphaFoldDB; I4EZV6; -.
DR STRING; 477641.MODMU_3507; -.
DR KEGG; mmar:MODMU_3507; -.
DR PATRIC; fig|477641.3.peg.3326; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_4_11; -.
DR OMA; MIDFRSD; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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:CCH88919.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 17..292
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 348 AA; 36263 MW; B18A122060C75BA0 CRC64;
MYGINTDGPA ASSGAVDLRS DTLTRPTPAM RRAMAEAEVG DDVYREDPTV NALEERVAEL
FGHEAALFVP SGTMGNQIGL RLVCEPGQEV LGDADAHILT YEMGAAAALF GLSSRTVVSA
GGRLSADQLI AQVRPHGDWH LTATAAVAVE NSHNRGGGLV QPLAELQRLF DWSRGAGVNV
HLDGARVFNA SVASGVPLST YGQLADTASV CLSKGLGAPI GSVLVASAER IAAGRLWRKR
LGGGMRQVGV LAAAGLHALD HHVERLAEDH EHARLLAERL GVDPATVETN MVVVQGVPAP
AVAEAAKAQG VLVGQVSADR IRLVTHLDVD RAGIEHAAKV VSQVIAEL
//
