ID A0A127FBZ4_STEDE Unreviewed; 433 AA.
AC A0A127FBZ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:AMN47140.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:AMN47140.1};
GN ORFNames=ACG33_08520 {ECO:0000313|EMBL:AMN47140.1};
OS Steroidobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Steroidobacterales;
OC Steroidobacteraceae; Steroidobacter.
OX NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN47140.1, ECO:0000313|Proteomes:UP000070250};
RN [1] {ECO:0000313|EMBL:AMN47140.1, ECO:0000313|Proteomes:UP000070250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN47140.1,
RC ECO:0000313|Proteomes:UP000070250};
RA Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W.,
RA Wang C.-H., Yang C.-Y., Chiang Y.-R.;
RT "A Comprehensive Approach to Explore the Metabolic and Phylogenetic
RT Diversity of Bacterial Steroid Degradation in the Environment: Testosterone
RT as an Example.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; CP011971; AMN47140.1; -; Genomic_DNA.
DR RefSeq; WP_066920364.1; NZ_CP011971.1.
DR AlphaFoldDB; A0A127FBZ4; -.
DR STRING; 465721.ACG33_08520; -.
DR KEGG; sdf:ACG33_08520; -.
DR PATRIC; fig|465721.4.peg.1813; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000070250; Chromosome.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AMN47140.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000070250}.
FT DOMAIN 2..78
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 97..379
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 108
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 433 AA; 47529 MW; D4259773D1776068 CRC64;
MQYISTRDET QKLTLSEAIA RGIAPDGGLY VPERFPRFLN SNFEGESEIA GIGPLLLAPF
AEDDSLADEL SVICREAFDF PVPLLPLEGA PAPASVLELF HGPTCAFKDI GARFLAACLQ
RIRKEAPRKL TILVATSGDT GGAVAAAFHD RPWVDVVVLY PKGLVSERQA QQLACWGGNV
RTFAVHGTFD DCQRMVKEAF QDPSLAQTHQ LSSANSINIG RLLPQMTYYA KAGLEVWRQT
GQRANFIIPT GNLGNALACL WARHVGLPIG EIVLATNANQ TITEYLHSGE WQPRASVPTL
ASAMDVGNPS NMERLRHLHA DFETLQGQVS AFSVDDTEIR STIRRDAHEL NQLWCPHSAT
AAEVFRRLIS RGARGHWVIV ATAHPAKFND IVEPHAGREV PVPSSLARLL ALPRQEMELQ
PTLQALRTQM QQV
//
