ID A0A0F3GNE3_9BACT Unreviewed; 410 AA.
AC A0A0F3GNE3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:KJU83455.1};
DE EC=4.2.3.- {ECO:0000313|EMBL:KJU83455.1};
GN ORFNames=MBAV_004355 {ECO:0000313|EMBL:KJU83455.1};
OS Candidatus Magnetobacterium bavaricum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetobacterium.
OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU83455.1, ECO:0000313|Proteomes:UP000033423};
RN [1] {ECO:0000313|EMBL:KJU83455.1, ECO:0000313|Proteomes:UP000033423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU83455.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-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}.
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:KJU83455.1}.
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DR EMBL; LACI01001889; KJU83455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3GNE3; -.
DR PATRIC; fig|29290.4.peg.5772; -.
DR Proteomes; UP000033423; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
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; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KJU83455.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000033423}.
FT DOMAIN 73..376
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 110
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 410 AA; 45065 MW; 2CCA266313E5FEBD CRC64;
MGFVVGLKCR ECAREYPIEP IYVCEFCFGP LEVVYDYEKI KNALTREKIL QREKNLWRYR
ELLPIDGEPQ VGLHSGFTPL VETKNLACAL GVKSLFVKDD TVVHPTLSFK DRVVAVALTK
AREFGFDTVS CASTGNLAHS VSAHGAKAGF KRFIFIPASL EASKIVASLV YEPNLIAVDG
NYDDVNRLCS EIANKYKWAF VNINIRPFYA EGSKTLGFET IEQLGWKAPD NVVVPCASGS
LLTKVWKSFK EFHEIGVLDN LHTRVFAAQA EGCNPIVSAI KSKIDVIRPI KPHTIAKSLA
IGNPADGYYA MKIIQETGGY GEDVTDDEII DGIQLLARTE GIFAETAGGV TVAVTRKLIE
QGVIGKDETT VICVTGNGLK TQEALAGKTV KPHHISPHMD SFEEVLNQIR
//
