(data stored in SCRATCH zone)

SWISSPROT: C1AT54_RHOOB

ID   C1AT54_RHOOB            Unreviewed;       439 AA.
AC   C1AT54;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
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:BAH48986.1};
GN   OrderedLocusNames=ROP_07390 {ECO:0000313|EMBL:BAH48986.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48986.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48986.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48986.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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: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; AP011115; BAH48986.1; -; Genomic_DNA.
DR   RefSeq; WP_012687985.1; NC_012522.1.
DR   STRING; 632772.ROP_07390; -.
DR   EnsemblBacteria; BAH48986; BAH48986; ROP_07390.
DR   KEGG; rop:ROP_07390; -.
DR   PATRIC; fig|632772.20.peg.802; -.
DR   eggNOG; ENOG4105CG0; Bacteria.
DR   eggNOG; COG0133; LUCA.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; DPFPRMV; -.
DR   OrthoDB; POG091H02JY; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002212; 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; C1AT54.
DR   SWISS-2DPAGE; C1AT54.
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:UP000002212};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00634273,
KW   ECO:0000313|EMBL:BAH48986.1};
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       81    405       PALP. {ECO:0000259|Pfam:PF00291}.
FT   MOD_RES     115    115       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00133}.
SQ   SEQUENCE   439 AA;  46586 MW;  79E9F387B61FAFDA CRC64;
     MTSRNQETVF KGGNLPTASA GIAERTTHDP DAGGHFGVYG GRHVPEALMA VIEEVTAEYE
     KARGDESFLN ELDRLQRDYT GRPSPIFEAT RMSEFAGGAR LILKREDLNH TGSHKINNVL
     GQVLLAKRMG KTRIIAETGA GQHGVATATA CALLGLECII YMGAVDTERQ ALNVARMRLL
     GSAVVSVESG SRTLKDAINE ALRDWVTNAH NTYYCFGTAA GPHPFPTIVR DFQRVVGLET
     RVQVQAATGR LPDAVTACVG GGSNAIGIFH AFLDDPSVRL VGYEAAGDGV ETGRHAATFA
     GGTPGAFQGA YSYLLQDEDG QTIESHSISA GLDYPGVGPE HALLKDIGRA TYEPVTDSEA
     MDALRLLSER EGIIPAIESA HAVAGALRLG RELGEGAIIV VSLSGRGDKD MDTAAKWFGL
     FDPDDSTETT TTDKEGSAK
//

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