(data stored in SCRATCH zone)

SWISSPROT: A4AT94_MARSH

ID   A4AT94_MARSH            Unreviewed;       393 AA.
AC   A4AT94;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN   OrderedLocusNames=FB2170_16306 {ECO:0000313|EMBL:EAR00664.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00664.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00664.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00541112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine =
CC         D-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;
CC         EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133,
CC         ECO:0000256|SAAS:SAAS01118361};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00133,
CC         ECO:0000256|SAAS:SAAS00166768};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00015996}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00345877}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00133, ECO:0000256|SAAS:SAAS00541094}.
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DR   EMBL; CP002157; EAR00664.1; -; Genomic_DNA.
DR   RefSeq; WP_013304467.1; NC_014472.1.
DR   STRING; 313603.FB2170_16306; -.
DR   EnsemblBacteria; EAR00664; EAR00664; FB2170_16306.
DR   KEGG; fbc:FB2170_16306; -.
DR   eggNOG; ENOG4105CG0; Bacteria.
DR   eggNOG; COG0133; LUCA.
DR   HOGENOM; HOG000161710; -.
DR   KO; K01696; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 912282at2; -.
DR   BioCyc; MSP313603:G1GNS-40-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06446; Trp-synth_B; 1.
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   PANTHER; PTHR42882; PTHR42882; 1.
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;
DR   PRODOM; A4AT94.
DR   SWISS-2DPAGE; A4AT94.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015918};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015879};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015853};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015971};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133,
KW   ECO:0000256|SAAS:SAAS00015947}.
FT   DOMAIN       55    378       PALP. {ECO:0000259|Pfam:PF00291}.
FT   MOD_RES      89     89       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00133}.
SQ   SEQUENCE   393 AA;  43080 MW;  8F5886432DDF2A35 CRC64;
     MSYNANERGY YGEFGGAFIP EMLYPNTEKL RLNYIRIMNE PSFKKEFDQL LKDYVGRPTP
     LYFAERLSKK YNTKIYLKRE DLCHTGAHKV NNTIGQILMA KKLGKKRIIA ETGAGQHGVA
     TATVCALMGI ECVVYMGEID IARQAPNVAR MKMLGAEVRP ALSGSRTLKD ATNEAIRDWI
     NNPVDTHYII GSVVGPHPYP DMVARFQSII SEEIKWQLME KEGVENPNYV VACVGGGSNA
     AGAFYHFLDN PDVGIIAVEA AGKGIDSGES AATSALGEVG IIHGSKTLLM QTKDGQITEP
     YSISAGLDYP GVGPMHAHLF KSGRGEFISI TDDEAMKAGL MICKLEGIIP AIESSHAFAI
     LDDKKFKPED VVVINLSGRG DKDLDTFIKY FDL
//

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