ID   N1MHX2_9SPHN            Unreviewed;       339 AA.
AC   N1MHX2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:CCW16820.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:CCW16820.1};
GN   ORFNames=EBBID32_11580 {ECO:0000313|EMBL:CCW16820.1};
OS   Sphingobium indicum BiD32.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW16820.1, ECO:0000313|Proteomes:UP000013201};
RN   [1] {ECO:0000313|EMBL:CCW16820.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW16820.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Le V.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW16820.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW16820.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Nielsen J.L., Zhou N.A., Kjeldal H.;
RT   "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:CCW16820.1}.
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DR   EMBL; CAVK010000057; CCW16820.1; -; Genomic_DNA.
DR   RefSeq; WP_006952263.1; NZ_CAVK010000057.1.
DR   AlphaFoldDB; N1MHX2; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000013201; Unassembled WGS sequence.
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; 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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CCW16820.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013201}.
FT   DOMAIN          3..288
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   339 AA;  35994 MW;  B3B890EAA3784080 CRC64;
     MHFFSDNATP VCPQVMAAMA AADRADHGYD GDQWSARLDG AFSALFDTQV RALWIATGTA
     ANSIALATLC PPYGGVICHE EAHIVVDECG APGFFTHGAS LMTLPGEGAK LSPDAVSDRL
     AIIRPDVHQV PARAISITNA TEYGRVYAPD EVAALGDIAR IRGLGFHMDG ARFANAVAHL
     GCTPADLTWR AGVDALSFGC VKNGGMIGEA LLFFGPEADA RAAEAARWRK RSGHLFSKGR
     YLAAQILAMV EDDLWLTNAR AANQAAQALA QAVADRLLHP VQANELFIRL TAQEAATLRA
     QDFDFYDWGE GAVRLVTNWS QDAAGVAPLA AALRALDHG
//