TRPB_AGRFC
ID TRPB_AGRFC Reviewed; 406 AA.
AC Q8UJB0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=Atu0018; ORFNames=AGR_C_28;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK85843.2; -; Genomic_DNA.
DR PIR; AC2579; AC2579.
DR PIR; B97361; B97361.
DR RefSeq; NP_353058.2; NC_003062.2.
DR RefSeq; WP_010970606.1; NC_003062.2.
DR AlphaFoldDB; Q8UJB0; -.
DR SMR; Q8UJB0; -.
DR STRING; 176299.Atu0018; -.
DR EnsemblBacteria; AAK85843; AAK85843; Atu0018.
DR KEGG; atu:Atu0018; -.
DR PATRIC; fig|176299.10.peg.19; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_5; -.
DR OMA; HGMKSYF; -.
DR PhylomeDB; Q8UJB0; -.
DR BioCyc; AGRO:ATU0018-MON; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000813; Chromosome circular.
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; 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 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;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..406
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000098909"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 43828 MW; D43AEA52DCAC0B38 CRC64;
MNDAPTPNSF RAGPDEDGRF GIYGGRFVAE TLMPLILDLQ AEWDKAKSDP EFQAELKYLG
THYTGRPSPL YFAERLTAEL GGAKIYFKRE ELNHTGSHKI NNCLGQILLA KRMGKTRIIA
ETGAGQHGVA SATVAARFGL PCVVYMGATD VARQAPNVFR MKLLGAEVKP VTAGHGTLKD
AMNEALRDWV TNVDDTYYLI GTAAGPHPYP EMVRDFQAVI GEEAKAQMLE AEGRLPDMII
AAVGGGSNAI GIFHPFLDDK NVRIVGVEAG GKGLSGEEHC ASITAGSPGV LHGNRTYLLQ
DGDGQIKEGH SISAGLDYPG IGPEHSWLND IGRVEYVPIM DHEALDAFQM LTRLEGIIPA
LEPSHALAEV IKRAPKMGKD EIILMNLSGR GDKDVHTVSK FLGMDV