(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBW4_SEGRD

ID   D6ZBW4_SEGRD            Unreviewed;       414 AA.
AC   D6ZBW4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
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   OrderedLocusNames=Srot_0454 {ECO:0000313|EMBL:ADG96941.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96941.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96941.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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:SAAS00541112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine =
CC         D-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;
CC         EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133,
CC         ECO:0000256|SAAS:SAAS01118361};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00133,
CC         ECO:0000256|SAAS:SAAS00166768};
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:SAAS00015996}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00345877}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00541094}.
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DR   EMBL; CP001958; ADG96941.1; -; Genomic_DNA.
DR   RefSeq; WP_013137397.1; NC_014168.1.
DR   STRING; 640132.Srot_0454; -.
DR   EnsemblBacteria; ADG96941; ADG96941; Srot_0454.
DR   KEGG; srt:Srot_0454; -.
DR   eggNOG; ENOG4105CG0; Bacteria.
DR   eggNOG; COG0133; LUCA.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 912282at2; -.
DR   BioCyc; SROT640132:G1GLH-454-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06446; Trp-synth_B; 1.
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   PANTHER; PTHR42882; PTHR42882; 1.
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; D6ZBW4.
DR   SWISS-2DPAGE; D6ZBW4.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015918};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015879};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015853};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015971};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015947}.
FT   DOMAIN       72    397       PALP. {ECO:0000259|Pfam:PF00291}.
FT   MOD_RES     107    107       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00133}.
SQ   SEQUENCE   414 AA;  44125 MW;  5BC1426B8C3DE57A CRC64;
     MSPAQPLPTA SEGVRVRTEH DPDAGGYFGR FGGRHVPEAL MAVIEEVTDA YEKARVDEDY
     LAQLDALQRD YVGRPSPLYE AKRLSEHAGG ARILLKREDL NHTGSHKINN VLGQGLLAKK
     MGKTRVIAET GAGQHGVATA TACALLGLEC VIYMGETDTE RQSLNVARMR LLGAHVMAVK
     TGSRTLKDAI NAALRDWVTN AATTYYCFGT AAGPHPFPMM VRDLQRVVGL ETRAQVREHV
     GQLPDAVVAC VGGGSNAIGI FDPFLRYRQV QLVGCEPAGD GVDTERHAAT LGGGSEGVFQ
     GSFSYLLQDQ DGQTVESHSI SAGLDYPGVG PQHAHLKETG RARYLPITDA QAMEAFDVLC
     RTEGIIPAIE SAHAVAGGLL LGRELGGGSV IVVNLSGRGD KDVDTAAKWF GMDL
//

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