ID TRPB_ACTSZ Reviewed; 398 AA.
AC A6VPD9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 30-NOV-2016, entry version 60.
DE RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133};
GN OrderedLocusNames=Asuc_1478;
OS Actinobacillus succinogenes (strain ATCC 55618 / 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes
RT for industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
CC {ECO:0000255|HAMAP-Rule:MF_00133}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000255|HAMAP-Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
DR EMBL; CP000746; ABR74836.1; -; Genomic_DNA.
DR RefSeq; WP_012073213.1; NC_009655.1.
DR ProteinModelPortal; A6VPD9; -.
DR STRING; 339671.Asuc_1478; -.
DR EnsemblBacteria; ABR74836; ABR74836; Asuc_1478.
DR KEGG; asu:Asuc_1478; -.
DR PATRIC; 20761334; VBIActSuc117883_1542.
DR eggNOG; ENOG4105CG0; Bacteria.
DR eggNOG; COG0133; LUCA.
DR HOGENOM; HOG000161710; -.
DR KO; K01696; -.
DR OMA; CQKEGII; -.
DR OrthoDB; POG091H02JY; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001114; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06446; Trp-synth_B; 1.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PLP-dep.
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;
KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1 398 Tryptophan synthase beta chain.
FT /FTId=PRO_1000076377.
FT MOD_RES 88 88 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000255|HAMAP-Rule:MF_00133}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 53 378 ipfam:PALP [T]
FT MYHIT 81 95 ipat:TRP_SYNTHASE_BETA [T]
FT MYHIT 1 392 ihamap:Trp_synth_beta [T]
SQ SEQUENCE 398 AA; 43502 MW; 0CAF4EBE53F7D378 CRC64;
MSDTILNPYF GEFGGMYVPE ILVPVLQQLE KAFVEARNDP DFQQEFQDLL KNYAGRPTAL
TLCRNLTKGT KTKLYLKRED LLHGGAHKTN QVLGQILLAK RMGKTRIIAE TGAGQHGVAT
ALACAMLDMP CRVYMGSKDV ERQSPNVFRM RLMGTEVVPV EKGSCSLKDA CCEAMRDWSA
NYENTHYLLG TAAGPHPFPT IVREFQKMIG EETKRQILEK EGCLPDAVIA AVGGGSNAIG
MFTDFIDETN VRLIGVEPAG KGIETGEHGA PLKHGKTGIY FGMKSPIMQT EDGQIEESYS
ISAGLDFPSV GPQHAYLNSI GRAEYPSITD DEALAAFKEL AKHEGIIPAL ESSHALAQAL
KMIKSNPEKE QLLVVNLSGR GDKDIFTVDK ILRAKGEL
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