TRPB_BACAN
ID TRPB_BACAN Reviewed; 397 AA.
AC Q81TL8; Q6I1U8; Q6KVP0;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 132.
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};
GN OrderedLocusNames=BA_1253, GBAA_1253, BAS1161;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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; AE016879; AAP25211.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30343.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53483.1; -; Genomic_DNA.
DR RefSeq; NP_843725.1; NC_003997.3.
DR RefSeq; WP_001105001.1; NZ_WXXJ01000020.1.
DR RefSeq; YP_027432.1; NC_005945.1.
DR PDB; 4NEG; X-ray; 2.20 A; A/B=1-397.
DR PDBsum; 4NEG; -.
DR AlphaFoldDB; Q81TL8; -.
DR SMR; Q81TL8; -.
DR IntAct; Q81TL8; 4.
DR STRING; 261594.GBAA_1253; -.
DR DNASU; 1086833; -.
DR EnsemblBacteria; AAP25211; AAP25211; BA_1253.
DR EnsemblBacteria; AAT30343; AAT30343; GBAA_1253.
DR GeneID; 45021253; -.
DR KEGG; ban:BA_1253; -.
DR KEGG; bar:GBAA_1253; -.
DR KEGG; bat:BAS1161; -.
DR PATRIC; fig|198094.11.peg.1229; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_9; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..397
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000098914"
FT MOD_RES 91
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:4NEG"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 201..224
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 333..347
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 353..365
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:4NEG"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:4NEG"
FT HELIX 387..393
FT /evidence="ECO:0007829|PDB:4NEG"
SQ SEQUENCE 397 AA; 43590 MW; 0C56E4584F798313 CRC64;
MNYAYPDEKG HYGIYGGRYV PETLMQSVLE LEEAYKEAME DEAFQKELNH YLKTYVGRET
PLYFAENMTE YCGGAKIYLK REDLNHTGAH KINNTIGQAL LAVRMGKKKV VAETGAGQHG
VATATVCALL GLECVIFMGE EDVRRQKLNV FRMELLGAKV ESVAAGSGTL KDAVNEALRY
WVSHVHDTHY IMGSVLGPHP FPQIVRDFQS VIGNETKKQY EALEGKLPEA VVACIGGGSN
AMGMFYPFVH DEEVALYGVE AAGKGVHTEK HAATLTKGSV GVLHGSMMYL LQNEEGQIQE
AHSISAGLDY PGVGPEHSLL KDIGRVSYHS ITDDEALEAF QLLTKKEGII PALESSHAVA
YALKLAPQMK EDEGLVICLS GRGDKDVESI KRYMEEV
