ID A0A098TML4_9CYAN Unreviewed; 420 AA.
AC A0A098TML4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN Name=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN ORFNames=DO97_12425 {ECO:0000313|EMBL:KGF72068.1};
OS Neosynechococcus sphagnicola sy1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC Neosynechococcaceae; Neosynechococcus.
OX NCBI_TaxID=1497020 {ECO:0000313|EMBL:KGF72068.1, ECO:0000313|Proteomes:UP000030170};
RN [1] {ECO:0000313|EMBL:KGF72068.1, ECO:0000313|Proteomes:UP000030170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAUP A 1101 {ECO:0000313|EMBL:KGF72068.1,
RC ECO:0000313|Proteomes:UP000030170};
RA Dvorak P., Casamatta D., Hasler P., Poulickova A., Ondrej V., Sanges R.;
RT "Evolution of Synechococcus.";
RL Mol. Ecol. 0:0-0(2014).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000003, ECO:0000256|HAMAP-
CC Rule:MF_00133};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00133};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|ARBA:ARBA00009982,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
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:KGF72068.1}.
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DR EMBL; JJML01000039; KGF72068.1; -; Genomic_DNA.
DR RefSeq; WP_036534945.1; NZ_JJML01000039.1.
DR AlphaFoldDB; A0A098TML4; -.
DR STRING; 1497020.DO97_12425; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000030170; Unassembled WGS sequence.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00263; trpB; 1.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00133};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00133};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00133}; Reference proteome {ECO:0000313|Proteomes:UP000030170};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 72..401
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 420 AA; 45619 MW; 13CACCEC5C77D3E4 CRC64;
MTLTPLPIPQ PQPLHSSPAQ PDALGRFGQF GGKYVPETLM PALSELEAAY QRYQIDPEFQ
QQLQGLLRDY VGRPTPLYFA ERLSDRYRRA DGTGPQIYLK REDLNHTGAH KINNALGQVL
LAKRMGKQRI IAETGAGQHG VATATVCARF GLECQIYMGV HDMERQALNV FRMRLMGAEV
RPVTAGTGTL KDATSEAIRD WVTHVETTHY ILGSVAGPHP YPMIVRDFQA IIGQETRSQC
QTLWGGLPDI LLACIGGGSN AMGLFHEFVQ EPSVRLIGVE AAGSGIETGK HAATLTQGRV
GVLHGAMSYL LQDSEGQVIE AHSISAGLDY PGVGPEHSYL KDLGRADYYS VTDQEALAGF
QRLSRLEGII PALETAHAIA YLETLCPQLT GSPRIVLNCS GRGDKDVQTV AKYLGDGMNA
//
