TRPB_MYCTU
ID TRPB_MYCTU Reviewed; 421 AA.
AC P9WFX9; L0T779; O08376; P66984;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 48.
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=Rv1612;
GN ORFNames=MTCY01B2.04;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP PROTEIN SEQUENCE OF 2-11, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP44376.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP44376.1; ALT_INIT; Genomic_DNA.
DR PIR; B70557; B70557.
DR RefSeq; NP_216128.1; NC_000962.3.
DR PDB; 2O2E; X-ray; 2.20 A; A/B=40-415.
DR PDB; 2O2J; X-ray; 2.56 A; A/B=40-415.
DR PDB; 5OCW; X-ray; 4.00 A; B/D/F/H/J/L/N/P/R/T/V/X=20-418.
DR PDB; 5TCF; X-ray; 2.46 A; B/D/F/H=16-420.
DR PDB; 5TCG; X-ray; 2.40 A; B/D/F/H=20-418.
DR PDB; 5TCH; X-ray; 2.35 A; B/D/F/H=16-420.
DR PDB; 5TCI; X-ray; 2.45 A; B/D/F/H=16-420.
DR PDB; 5TCJ; X-ray; 2.40 A; B/D/F/H=20-418.
DR PDB; 6DWE; X-ray; 2.69 A; B/D/F/H=16-419.
DR PDB; 6E9P; X-ray; 2.57 A; B/D/F/H=16-420.
DR PDB; 6U6C; X-ray; 2.40 A; B/D/F/H=15-419.
DR PDB; 6UAP; X-ray; 2.75 A; B/D/F/H=16-420.
DR PDB; 6UB9; X-ray; 2.78 A; B/D/F/H=16-419.
DR PDB; 6USA; X-ray; 2.41 A; B/D/F/H=16-419.
DR PDBsum; 2O2E; -.
DR PDBsum; 2O2J; -.
DR PDBsum; 5OCW; -.
DR PDBsum; 5TCF; -.
DR PDBsum; 5TCG; -.
DR PDBsum; 5TCH; -.
DR PDBsum; 5TCI; -.
DR PDBsum; 5TCJ; -.
DR PDBsum; 6DWE; -.
DR PDBsum; 6E9P; -.
DR PDBsum; 6U6C; -.
DR PDBsum; 6UAP; -.
DR PDBsum; 6UB9; -.
DR PDBsum; 6USA; -.
DR AlphaFoldDB; P9WFX9; -.
DR SMR; P9WFX9; -.
DR STRING; 83332.Rv1612; -.
DR PaxDb; P9WFX9; -.
DR DNASU; 885297; -.
DR GeneID; 885297; -.
DR KEGG; mtu:Rv1612; -.
DR PATRIC; fig|83332.12.peg.1794; -.
DR TubercuList; Rv1612; -.
DR eggNOG; COG0133; Bacteria.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004834; F:tryptophan synthase activity; IDA:MTBBASE.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:MTBBASE.
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 Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW Tryptophan biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..421
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000098969"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:2O2E"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:2O2E"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2O2J"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:2O2E"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5TCH"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:5TCH"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 375..391
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:2O2E"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2O2E"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:2O2E"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:5TCH"
SQ SEQUENCE 421 AA; 44514 MW; FB00A3153CA8F7BC CRC64;
MTDLSTPDLP RMSAAIAEPT SHDPDSGGHF GGPSGWGGRY VPEALMAVIE EVTAAYQKER
VSQDFLDDLD RLQANYAGRP SPLYEATRLS QHAGSARIFL KREDLNHTGS HKINNVLGQA
LLARRMGKTR VIAETGAGQH GVATATACAL LGLDCVIYMG GIDTARQALN VARMRLLGAE
VVAVQTGSKT LKDAINEAFR DWVANADNTY YCFGTAAGPH PFPTMVRDFQ RIIGMEARVQ
IQGQAGRLPD AVVACVGGGS NAIGIFHAFL DDPGVRLVGF EAAGDGVETG RHAATFTAGS
PGAFHGSFSY LLQDEDGQTI ESHSISAGLD YPGVGPEHAW LKEAGRVDYR PITDSEAMDA
FGLLCRMEGI IPAIESAHAV AGALKLGVEL GRGAVIVVNL SGRGDKDVET AAKWFGLLGN
D
