ID B1A7I5_FLAPS Unreviewed; 311 AA.
AC B1A7I5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
DE Flags: Fragment;
GN Name=trpB {ECO:0000313|EMBL:ABZ88622.1};
OS Flavobacterium psychrophilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=96345 {ECO:0000313|EMBL:ABZ88622.1};
RN [1] {ECO:0000313|EMBL:ABZ88622.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LFNW 131/89 {ECO:0000313|EMBL:ABZ88622.1}, and LVDJ H9480
RC {ECO:0000313|EMBL:ABZ88635.1};
RC TISSUE=Kidney {ECO:0000313|EMBL:ABZ88622.1};
RX PubMed=18424537; DOI=10.1128/AEM.00244-08;
RA Nicolas P., Mondot S., Achaz G., Bouchenot C., Bernardet J.F., Duchaud E.;
RT "Population structure of the fish-pathogenic bacterium Flavobacterium
RT psychrophilum.";
RL Appl. Environ. Microbiol. 74:3702-3709(2008).
RN [2] {ECO:0000313|EMBL:AGA17519.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=09/360 {ECO:0000313|EMBL:AGA17519.1};
RC TISSUE=Skin {ECO:0000313|EMBL:AGA17519.1};
RA Strepparava N., Nicolas P., Wahli T., Segner H., Petrini O.;
RT "Molecular epidemiology of Flavobacterium psychrophilum from Swiss fish
RT farms.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000003};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270}.
CC -!- SIMILARITY: Belongs to the TrpB family.
CC {ECO:0000256|ARBA:ARBA00009982}.
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DR EMBL; EU428664; ABZ88622.1; -; Genomic_DNA.
DR EMBL; EU428677; ABZ88635.1; -; Genomic_DNA.
DR EMBL; JX880123; AGA17519.1; -; Genomic_DNA.
DR AlphaFoldDB; B1A7I5; -.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:InterPro.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
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_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00263; trpB; 1.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 1..306
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABZ88622.1"
FT NON_TER 311
FT /evidence="ECO:0000313|EMBL:ABZ88622.1"
SQ SEQUENCE 311 AA; 33722 MW; 08442641ED15222F CRC64;
TPLYFAERLS KEYNTKIYLK REDLCHTGAH KVNNTIGQIL LAKRLGKTRI IAETGAGQHG
VATATVCALM GLQCIVYMGE IDIKRQAPNV ARMKMLGAEV RPATSGSKTL KDATNEAIRD
WINNPTNTYY IIGSVVGPHP YPDMVARFQS VISQEIKTQL LEKEGQENPD YIIACVGGGS
NAAGAFYHFL DEKEVNIIAV EAAGKGIYSG ESAATSALGK IGIIHGSKTL LMQSPDGQIT
EPYSISAGLD YPGVGPMHAH LFETKRAQFI SITDDQAMNW GIKMSQTEGI IPAIESAHAF
AVLDHKKFKP T
//