TRPA_BACSU
ID TRPA_BACSU Reviewed; 267 AA.
AC P07601; Q59793;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; OrderedLocusNames=BSU22630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3924737; DOI=10.1016/0378-1119(85)90125-8;
RA Henner D.J., Band L., Shimotsu H.;
RT "Nucleotide sequence of the Bacillus subtilis tryptophan operon.";
RL Gene 34:169-177(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-182.
RC STRAIN=K;
RX PubMed=7763866; DOI=10.1271/bbb.57.1006;
RA Kurahashi O., Kawashima H., Nakamori S., Yamane K.;
RT "Cloning and nucleotide sequence of the Bacillus subtilis K trpB gene
RT encoding tryptophan synthase beta-subunit.";
RL Biosci. Biotechnol. Biochem. 57:1006-1009(1993).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
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_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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; M80245; AAA20866.1; -; Genomic_DNA.
DR EMBL; K01391; AAA22870.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14179.1; -; Genomic_DNA.
DR EMBL; S65045; AAC60451.2; -; Genomic_DNA.
DR PIR; F22794; F22794.
DR RefSeq; NP_390144.1; NC_000964.3.
DR RefSeq; WP_003230608.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P07601; -.
DR SMR; P07601; -.
DR STRING; 224308.BSU22630; -.
DR PaxDb; P07601; -.
DR PRIDE; P07601; -.
DR EnsemblBacteria; CAB14179; CAB14179; BSU_22630.
DR GeneID; 939011; -.
DR KEGG; bsu:BSU22630; -.
DR eggNOG; COG0159; Bacteria.
DR InParanoid; P07601; -.
DR OMA; LVMTYWN; -.
DR PhylomeDB; P07601; -.
DR BioCyc; BSUB:BSU22630-MON; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..267
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098744"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT CONFLICT 1..8
FT /note="MFKLDLQP -> MFNLHD (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="V -> L (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..28
FT /note="VSI -> ISV (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="K -> N (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="T -> S (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="L -> I (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..49
FT /note="AYS -> PYT (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..68
FT /note="DQ -> EN (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="E -> K (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="N -> H (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..107
FT /note="QLNKEY -> ELEKEC (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="H -> D (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..132
FT /note="NS -> AL (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..143
FT /note="EECKSHEVT -> KTCKKENIA (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> N (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..160
FT /note="TII -> IIT (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> G (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="N -> S (in Ref. 3; AAC60451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29450 MW; BFC804E410B042DD CRC64;
MFKLDLQPSE KLFIPFITAG DPVPEVSIEL AKSLQKAGAT ALELGVAYSD PLADGPVIQR
ASKRALDQGM NIVKAIELGG EMKKNGVNIP IILFTYYNPV LQLNKEYFFA LLRENHIDGL
LVPDLPLEES NSLQEECKSH EVTYISLVAP TSESRLKTII EQAEGFVYCV SSLGVTGVRN
EFNSSVYPFI RTVKNLSTVP VAVGFGISNR EQVIKMNEIS DGVVVGSALV RKIEELKDRL
ISAETRNQAL QEFEDYAMAF SGLYSLK
