TRPB_ACIAD
ID TRPB_ACIAD Reviewed; 403 AA.
AC Q6FEF1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=ACIAD0636;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67557.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6FEF1; -.
DR SMR; Q6FEF1; -.
DR STRING; 62977.ACIAD0636; -.
DR EnsemblBacteria; CAG67557; CAG67557; ACIAD0636.
DR KEGG; aci:ACIAD0636; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_6; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000430; 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..403
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018317"
FT MOD_RES 93
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 403 AA; 44322 MW; 2B4AA1F3EE46E357 CRC64;
MIDYTQYPDA RGHFGIHGGR FVSETLMAAL EDLENLYNRM KNDEQFLAEF DRDLAYYVGR
PSPLYYAERW SKKLGGAQIY LKREDLNHTG SHKVNNTIGQ ALLAKLSGKK RIIAETGAGQ
HGVATATIAA RLGLECVVFM GAEDVKRQAM NVYRMRLLGA TVIPVQSGSK TLKDAMNEAM
RDWVTNVDST YYVIGTVAGP HPYPQLVRDF QSIIGREARR QIQEQAGRLP DALVACVGGG
SNAIGLFYPF LNDQDVKMYG VEAAGHGIET GKHSAPLNAG HVGVLHGNRT YLMSDPQGQI
IETHSISAGL DYPGVGPEHS FLKDMHRVEY VPIDDNEALQ GFRDLTRIEG IIPAIESAHA
MAYVTKLAPT MDKDQIIIAN VSGRGDKDLM TVARIDGIEM VEM