TRPB_META3
ID TRPB_META3 Reviewed; 389 AA.
AC A6UW25;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Maeo_1120;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000743; ABR56697.1; -; Genomic_DNA.
DR RefSeq; WP_011973829.1; NC_009635.1.
DR AlphaFoldDB; A6UW25; -.
DR SMR; A6UW25; -.
DR STRING; 419665.Maeo_1120; -.
DR EnsemblBacteria; ABR56697; ABR56697; Maeo_1120.
DR GeneID; 5327416; -.
DR KEGG; mae:Maeo_1120; -.
DR eggNOG; arCOG01433; Archaea.
DR HOGENOM; CLU_016734_3_1_2; -.
DR OMA; GPEHAMF; -.
DR OrthoDB; 24741at2157; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001106; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..389
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018357"
FT MOD_RES 84
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 389 AA; 42775 MW; 8C253EBEAD8BC850 CRC64;
MEYKFGEYGG QYVPEVLMPS LKELEKAYKK YKDDPEFKEE LEYYLKQYAG RETPLYFAEN
LTKKMGGAKI YLKREDLLLG GAHKINNSLG QALLAKRIGK TRIIAETGAG EHGLSTAMVG
ALFGLKAKIY MGAVDVERQK LNVYKMRLHG AEVHAVQSGS KTLKDAINEA LRDWVETFED
THYIIGSAVG PYPFPSMVRD FQSVIGKEAK KQILEAEGRL PDSIVACVGG GSNSIGIFNE
FKQDKEVKLI GVEAAGEGLD TDRHGAAILK GKKGVLHGML SKFLQDDDGQ IAETYSISAG
LDYPGVGPEH AYLDEIKRVE YAGITDVEAL DAFSTLSKTE GIIPALESSH AVAHGMKIAK
EMDKDEIIII NLSGRGDKDI HTVMNFIEF