TRPB2_AQUAE
ID TRPB2_AQUAE Reviewed; 434 AA.
AC O67409;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Tryptophan synthase beta chain 2;
DE EC=4.2.1.20;
GN Name=trpB2; OrderedLocusNames=aq_1410;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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}.
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DR EMBL; AE000657; AAC07370.1; -; Genomic_DNA.
DR PIR; G70422; G70422.
DR RefSeq; NP_213974.1; NC_000918.1.
DR RefSeq; WP_010880912.1; NC_000918.1.
DR AlphaFoldDB; O67409; -.
DR SMR; O67409; -.
DR STRING; 224324.aq_1410; -.
DR PRIDE; O67409; -.
DR EnsemblBacteria; AAC07370; AAC07370; aq_1410.
DR KEGG; aae:aq_1410; -.
DR PATRIC; fig|224324.8.peg.1105; -.
DR eggNOG; COG1350; Bacteria.
DR HOGENOM; CLU_042858_1_0_0; -.
DR InParanoid; O67409; -.
DR OMA; MLHQTII; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0052684; F:L-serine hydro-lyase (adding indole, L-tryptophan-forming) activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..434
FT /note="Tryptophan synthase beta chain 2"
FT /id="PRO_0000098913"
FT MOD_RES 110
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 48314 MW; 7D1921128B07C39B CRC64;
MRKFLLSEGE IPKKWLNILP LLPEPLEPPL DPETMEPVKP EKLLAIFPEP LVEQEVSDKE
WIDIPEEVLD IYSLWRPTPL HRAKNLEEFL GTPAKIFYKN ESVSPPGSHK PNTAVAQAYY
NKISGVKRLT TETGAGQWGS ALSFATQFFD LQCRVYMVRV SYNQKPYRRI LMETWKGEVI
PSPSPYTNAG RKYYEENPEH PGSLGIAISE AIEEAASRED TKYSLGSVLN HVLLHQTVIG
LEAKKQMEEA GYYPDVIIGA VGGGSNFAGL SFPFLADVLR GDKRKEDLKV LAVEPEACPT
LTKGEYKYDF GDSVGLTPLI KMYTLGHDFV PSPIHAGGLR YHGDAPLVCK LYNLGYIDAV
AYKQTEVFEA AVTFARTEGI VPAPESAHAI KAAIDEALKC KETGEEKVIL FNLSGHGYFD
LSAYDKYLHG ELTD