TRPB_PROM0
ID TRPB_PROM0 Reviewed; 414 AA.
AC A3PAN2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133}; OrderedLocusNames=P9301_01841;
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00133};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
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DR EMBL; CP000576; ABO16807.1; -; Genomic_DNA.
DR RefSeq; WP_011862209.1; NC_009091.1.
DR AlphaFoldDB; A3PAN2; -.
DR SMR; A3PAN2; -.
DR STRING; 167546.P9301_01841; -.
DR EnsemblBacteria; ABO16807; ABO16807; P9301_01841.
DR KEGG; pmg:P9301_01841; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_3; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001430; Chromosome.
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; IPR001926; PLP-dep.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00263; trpB; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..414
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018368"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 414 AA; 45078 MW; 2583297343834C1F CRC64;
MVSTFSRKDQ NYKNDDLNQP SKEGRFGKYG GQYVPETLMP ALFELETAAS NAWKDKLFVE
ELNHLLKTYV GRETPLYEAK RLTEHYKTKQ ATPRIWLKRE DLNHTGAHKI NNALGQALLA
IRMGKKRIIA ETGAGQHGVA TATVCARFGL KCIIYMGAED IKRQSLNVFR MKLLGAEVKV
VNSGTATLKD ATSEAIRDWV SNVETTHYIL GSVAGPHPFP KIVRDFHAVI GEETKKQCLE
SFGSFPDILL ACVGGGSNAM GLFHPFVKET SVRLIGVEAA GSGVDTDKHA ATITKGSVGI
LHGSMSLLLQ DDNGQVQEAH SISAGLDYPG VGPEHSHLKE IGRAEYGSVT DQEALDALKL
VSELEGIIPA LETSHAFAWL DKLCPTLEKD THIVINCSGR GDKDVNTVAS SLDI