ID D7E191_NOSA0 Unreviewed; 434 AA.
AC D7E191;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:ADI64768.1};
GN OrderedLocusNames=Aazo_2960 {ECO:0000313|EMBL:ADI64768.1};
OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI64768.1, ECO:0000313|Proteomes:UP000001511};
RN [1] {ECO:0000313|EMBL:ADI64768.1, ECO:0000313|Proteomes:UP000001511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0708 {ECO:0000313|EMBL:ADI64768.1,
RC ECO:0000313|Proteomes:UP000001511};
RX PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT multicellular cyanobacterium.";
RL PLoS ONE 5:E11486-E11486(2010).
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; CP002059; ADI64768.1; -; Genomic_DNA.
DR RefSeq; WP_013191784.1; NC_014248.1.
DR AlphaFoldDB; D7E191; -.
DR STRING; 551115.Aazo_2960; -.
DR KEGG; naz:Aazo_2960; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_028142_4_1_3; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000001511; Chromosome.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000001511}.
FT DOMAIN 86..388
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 122
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 434 AA; 47199 MW; E9168CC4D9E8E7CF CRC64;
MTQAIANLNQ ANTSILKALK CKECGAEYEL QASHVCELCF GPLEVKYDYD VLRQSVSRKS
IETGPNSIWR YRHFLPITTD NYIDVGTGMT PLVRSQRLAR RLGLNKLYIK NDAVNMPTLS
FKDRVVTVAL SRARELGFTT VSCASTGNLA NSTAAIAAHA GLDCCVFIPA DLEAGKVLGS
LIYSPTLMAV KGNYDQVNRL CSEVANTHGW GFVNINLRPY YSEGSKTLGF EVAEQLGWEL
PDHIVAPLAS GSLFTKIYKG FKEFTEVGLL EGKNVRFSGA QAEGCSPIAT AFKEKRDFIQ
PVKPNTIAKS IAIGNPADGV YAVEIAQKTG GNIESVNDAE IINGIKLLAE TEGIFTETAG
GTTVAVLKKL VEAGKIDPDE TTVVYITGNG LKTQEAIQGY VGEPLTIDAK LDSFERALER
SRTLDRLEWQ QVLV
//
