位置:首页 > 蛋白库 > TRPB2_PYRAB
TRPB2_PYRAB
ID   TRPB2_PYRAB             Reviewed;         440 AA.
AC   Q9V150; G8ZJ44;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Tryptophan synthase beta chain 2;
DE            EC=4.2.1.20;
GN   Name=trpB2; Synonyms=trpB-2; OrderedLocusNames=PYRAB05790;
GN   ORFNames=PAB1970;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB49501.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AJ248284; CAB49501.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE69971.1; -; Genomic_DNA.
DR   PIR; F75177; F75177.
DR   RefSeq; WP_048146581.1; NC_000868.1.
DR   AlphaFoldDB; Q9V150; -.
DR   SMR; Q9V150; -.
DR   STRING; 272844.PAB1970; -.
DR   EnsemblBacteria; CAB49501; CAB49501; PAB1970.
DR   GeneID; 1495484; -.
DR   KEGG; pab:PAB1970; -.
DR   PATRIC; fig|272844.11.peg.617; -.
DR   eggNOG; arCOG01432; Archaea.
DR   HOGENOM; CLU_042858_1_0_2; -.
DR   OrthoDB; 24741at2157; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
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; IPR006316; Trp_synth_b-like.
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; PTHR48077:SF6; PTHR48077:SF6; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   PIRSF; PIRSF500824; TrpB_prok; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01415; trpB_rel; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Tryptophan biosynthesis.
FT   CHAIN           1..440
FT                   /note="Tryptophan synthase beta chain 2"
FT                   /id="PRO_0000099048"
FT   MOD_RES         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  48943 MW;  580BC102EBAB36F5 CRC64;
     MKVVLPDGRI PRRWYNILPD LPEPLDPPLD PETEEPIDIE KLKRIFAEEL VKQEISRERY
     IEIPGELRKL YSKIGRPTPL FRATNLEKLL GTPARIYFKY EGATVTGSHK INTALAQAYY
     AKKQGIERLV TETGAGQWGT ALSLAGALLG LKVRVYMARA SYQQKPYRKT LMRIYGAEVF
     PSPSENTEVG KRFLKEDPNH PGSLGIAISE AIEDVLKDEK ARYSLGSVLN HVLMHQTVIG
     LEAKEQMEEF EEPDVIIGCV GGGSNFAGLA YPFVKDVLDG KSEYEFIAVE PKAAPTMTRG
     VYTYDYGDSA GLTPKLKMHT LGHRYYVPPI HAGGLRYHGL APTLSVLINH GIVKPIAYHQ
     TEVFEAAVLF AKAEGIVPAP ESAHAVKAVI DKALEARREG KEMVILFNLS GHGLLDLKGY
     EDYLDGKLED YEPRDLPVKS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024