ID A0A0B5DCW1_9CORY Unreviewed; 448 AA.
AC A0A0B5DCW1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=B842_10945 {ECO:0000313|EMBL:AJE34038.1};
OS Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE34038.1, ECO:0000313|Proteomes:UP000031524};
RN [1] {ECO:0000313|EMBL:AJE34038.1, ECO:0000313|Proteomes:UP000031524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT isolated from a wastewater-fed microbial fuel cell.";
RL Submitted (APR-2013) 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: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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP005286; AJE34038.1; -; Genomic_DNA.
DR RefSeq; WP_052437901.1; NZ_CP005286.1.
DR AlphaFoldDB; A0A0B5DCW1; -.
DR STRING; 1223515.B842_10945; -.
DR KEGG; chm:B842_10945; -.
DR HOGENOM; CLU_016734_3_1_11; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000031524; 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; 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};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 73..399
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 448 AA; 48230 MW; A19E2A7526B8F245 CRC64;
MNLTPRLHDN PEIPAGEARE TILPAYFGKF GGQFVPPMLY PVLDELERAY AEALEDEEFI
AELDKLYRSY LGRPTPVTEC VNLPREGKGR GHARIFLKRE DLVHGGAHKG NQVMAQALLA
KKLGKTRLIA ETGAGQHGTA TAMAAARFGM DCTIYMGARD IARQQANVYR MRLMGAEVVA
VDEDGGNGLQ NAVDVALLDW VESYETTHYL LGTAAGPHPF PSLVKEYHRV ISKESREQML
AEVGRLPDAV IAAVGGGSNA IGAFAEYYGD TDVQLIGAEP AGEGLDSGKH GAPLNRGRVG
ILHGSRSYVM LGEGDDDVLN SHSISAGLDY PGIGPEHAWL METGRATYVG ATDAEALQAF
RMLTRYEGII PALESSHALA HALKLAEQDE AEGRTDRVYL VNLSGRGDKD VNYVRRMLGD
AADLDPDTHG VEKLDVAGAI AALEAEAD
//
