TRPB_PROMT
ID TRPB_PROMT Reviewed; 417 AA.
AC Q46HK9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=PMN2A_1531;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
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; CP000095; AAZ59019.1; -; Genomic_DNA.
DR RefSeq; WP_011294164.1; NC_007335.2.
DR AlphaFoldDB; Q46HK9; -.
DR SMR; Q46HK9; -.
DR STRING; 59920.PMN2A_1531; -.
DR EnsemblBacteria; AAZ59019; AAZ59019; PMN2A_1531.
DR KEGG; pmn:PMN2A_1531; -.
DR HOGENOM; CLU_016734_3_1_3; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR PhylomeDB; Q46HK9; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002535; 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..417
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018373"
FT MOD_RES 110
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 417 AA; 45261 MW; 9C6A11550EEA2F66 CRC64;
MTGTLPTQFK DSDLSPLTRP NTLGRFGKYG GQYVPETLIP ALIELEQAAK EAWKDSSFNS
ELNHLLKTYV GRSTPLYEAT RLTEHYRKNT LKGPRIWLKR EDLNHTGAHK INNALGQALL
AIRMGKKRII AETGAGQHGV ATATVCARFG LECIIYMGKE DMRRQALNVF RMQLLGASVR
PVTSGTATLK DATSEAIRDW VTNVETTHYI LGSVAGPHPY PMLVRDFHAV IGEETKQQCK
QAFGRSPDVL LACVGGGSNA MGLFHSFVED KSVRMIGVEA AGDGVETGRH AATITEGRIG
VLHGAMSLLL QDKDGQVEEA HSISAGLDYP GVGPEHSYLK EIGRAEYAAV TDTEAIEALQ
LVSKLEGIIP ALETAHAFAY LEKLCPTLNH NSEIVINCSG RGDKDVNTVA EKLGSEI