TRPB2_ARCFU
ID TRPB2_ARCFU Reviewed; 435 AA.
AC O29028;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Tryptophan synthase beta chain 2;
DE EC=4.2.1.20;
GN Name=trpB2; OrderedLocusNames=AF_1240;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB90007.1; -; Genomic_DNA.
DR PIR; G69404; G69404.
DR AlphaFoldDB; O29028; -.
DR SMR; O29028; -.
DR STRING; 224325.AF_1240; -.
DR EnsemblBacteria; AAB90007; AAB90007; AF_1240.
DR KEGG; afu:AF_1240; -.
DR eggNOG; arCOG01432; Archaea.
DR HOGENOM; CLU_042858_1_0_2; -.
DR OMA; MLHQTII; -.
DR PhylomeDB; O29028; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002199; 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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..435
FT /note="Tryptophan synthase beta chain 2"
FT /id="PRO_0000099033"
FT MOD_RES 115
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 48011 MW; 78595BEF6B42D44B CRC64;
MLSWCMKKIM LDESEMPKEW YNVLPDLPEP LPPPLHPATQ EPVKPEDLEP IFPKGLIQQE
MSGERWIRIP EDVREIYRIW RPTPLVRAER LEKALKTPAR IYFKYEGASP PGSHKPNTAV
AQAYYNAKEG VERLTTETGA GQWGSALCFA TKLFEMACTV YMVKVSFMQK PYRRVMMETW
GGEVIPSPSD RTEVGRKILA ENPDTPGSLG IAISEAIEDA AKNENTKYSL GSVLNHVLLH
QTVIGLETKA QLEKVDEKPD VLIGCVGGGS NFAGLTYPFV NDAKNGDLEI IAVEPAACPT
LTAGEYKYDF GDVAGLTPLL KMYTLGHDFI PPPIHAGGLR YHGDAPTLCM LVKHGVIKAR
AVKQLPTFEA GLLFARTEGI IPAPETNHAV RAAIDEAIKA RENNEEKVIV FGFSGHGLLD
LQAYDDYLAG RLADT