ID F8QZ32_FLAPS Unreviewed; 277 AA.
AC F8QZ32;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:ADQ13009.1};
OS Flavobacterium psychrophilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=96345 {ECO:0000313|EMBL:ADQ13009.1};
RN [1] {ECO:0000313|EMBL:ADQ13009.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FLpR 010/09 {ECO:0000313|EMBL:ADQ13009.1};
RA Dyrkorn Loland A., Nylund A., Brevik O.J.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ13009.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FLpR 010/09 {ECO:0000313|EMBL:ADQ13009.1};
RX PubMed=23289591; DOI=10.1111/jam.12121;
RA Apablaza P., Loland A.D., Brevik O.J., Ilardi P., Battaglia J., Nylund A.;
RT "Genetic variation among Flavobacterium psychrophilum isolates from wild
RT and farmed salmonids in Norway and Chile.";
RL J. Appl. Microbiol. 114:934-946(2013).
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; HM443851; ADQ13009.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QZ32; -.
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..271
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADQ13009.1"
FT NON_TER 277
FT /evidence="ECO:0000313|EMBL:ADQ13009.1"
SQ SEQUENCE 277 AA; 29941 MW; F37AF14EF1943C52 CRC64;
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 GIKMSQT
//
