TRPB_CHLTR
ID TRPB_CHLTR Reviewed; 392 AA.
AC O84172;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=CT_170;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
CC -!- CAUTION: This TrpB is highly divergent compared to other bacterial
CC TrpB. As C.trachomatis seems to have lost part of the Trp biosynthetic
CC operon, it is possible that this protein is not active. {ECO:0000305}.
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DR EMBL; AE001273; AAC67761.1; -; Genomic_DNA.
DR PIR; A71547; A71547.
DR RefSeq; NP_219673.1; NC_000117.1.
DR RefSeq; WP_009873061.1; NC_000117.1.
DR PDB; 6V82; X-ray; 2.42 A; B=1-392.
DR PDBsum; 6V82; -.
DR AlphaFoldDB; O84172; -.
DR SMR; O84172; -.
DR STRING; 813.O172_00910; -.
DR EnsemblBacteria; AAC67761; AAC67761; CT_170.
DR GeneID; 884961; -.
DR KEGG; ctr:CT_170; -.
DR PATRIC; fig|272561.5.peg.183; -.
DR HOGENOM; CLU_016734_3_1_0; -.
DR InParanoid; O84172; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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..392
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000098941"
FT MOD_RES 84
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:6V82"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 326..340
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6V82"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6V82"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:6V82"
SQ SEQUENCE 392 AA; 42618 MW; 3340FECFFF9880BF CRC64;
MFKHKHPFGG AFLPEELLAP IQNLKAEWEI LKTQQSFLSE LDCILKNYAG RQTPLTEVKN
FARAIDGPRV FLKREDLLHT GAHKLNNALG QCLLAKYLGK TRVVAETGAG QHGVATATAC
AYLGLDCVVY MGAKDVERQK PNVEKMRFLG AEVVSVTKGS CGLKDAVNQA LQDWATTHSF
THYCLGSALG PLPYPDIVRF FQSVISAEVK EQIHAVAGRD PDILIACIGG GSNAIGFFHH
FIPNPKVQLI GVEGGGLGIS SGKHAARFAT GRPGVFHGFY SYLLQDDDGQ VLQTHSISAG
LDYPSVGPDH AEMHESGRAF YTLATDEEAL RAFFLLTRNE GIIPALESSH ALAHLVSIAP
SLPKEQIVIV NLSGRGDKDL PQIIRRNRGI YE
