(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZK36_PSEAB

ID   A0A0H2ZK36_PSEAB        Unreviewed;       402 AA.
AC   A0A0H2ZK36;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 14.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000256|HAMAP-Rule:MF_00133,
GN   ECO:0000313|EMBL:ABJ14993.1};
GN   OrderedLocusNames=PA14_00450 {ECO:0000313|EMBL:ABJ14993.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ14993.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ14993.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ14993.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00634256}.
CC   -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC       phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
CC       {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00634297}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00133,
CC         ECO:0000256|SAAS:SAAS00634278};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00634294}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00634300}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00634293}.
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DR   EMBL; CP000438; ABJ14993.1; -; Genomic_DNA.
DR   RefSeq; WP_003142212.1; NC_008463.1.
DR   EnsemblBacteria; ABJ14993; ABJ14993; PA14_00450.
DR   KEGG; pau:PA14_00450; -.
DR   KO; K01696; -.
DR   OMA; DPFPRMV; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
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;
DR   PRODOM; A0A0H2ZK36.
DR   SWISS-2DPAGE; A0A0H2ZK36.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00634295};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00634252};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00634273};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00634284};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00634298}.
FT   DOMAIN       58    383       PALP. {ECO:0000259|Pfam:PF00291}.
FT   MOD_RES      93     93       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00133}.
SQ   SEQUENCE   402 AA;  43694 MW;  CC3A2B73E1EBC8FC CRC64;
     MTSYRNGPDA KGLFGRFGGQ YVAETLMPLI LDLAREYEKA KDDPAFQEEL AYFQRDYVGR
     PSPLYFAERL TEHCGGAKIY LKREELNHTG AHKINNCIGQ ILLARRMGKK RIIAETGAGM
     HGVATATVAA RFGLQCVIYM GTTDIDRQQA NVFRMKLLGA EVIPVTAGTG TLKDAMNEAL
     RDWVTNVDST FYLIGTVAGP HPYPAMVRDF QAVIGKETRE QLAEKEGRLP NSLIACIGGG
     SNAMGLFHPF LDDAGVQIVG VEAAGHGIDT GKHAASLNGG VPGVLHGNRT FLLQDADGQI
     IDAHSISAGL DYPGIGPEHA WLHDTGRVEY TSITDDEALE AFHTCCRLEG IIPALESSHA
     LAEVFKRAPS LPKEHIMVVN LSGRGDKDMQ TVMHHMQQES KA
//

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