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Database: UniProt
Entry: A0A139DA73_9FIRM
LinkDB: A0A139DA73_9FIRM
Original site: A0A139DA73_9FIRM 
ID   A0A139DA73_9FIRM        Unreviewed;       394 AA.
AC   A0A139DA73;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ORFNames=AWL62_150 {ECO:0000313|EMBL:KXS50426.1};
OS   Halanaerobium sp. T82-1.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=1794808 {ECO:0000313|EMBL:KXS50426.1, ECO:0000313|Proteomes:UP000070487};
RN   [1] {ECO:0000313|EMBL:KXS50426.1, ECO:0000313|Proteomes:UP000070487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T82-1 {ECO:0000313|EMBL:KXS50426.1};
RA   Wolfe R., Daly R., Wrighton K.;
RT   "Halanaerobium-1 T82 Annotated.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00133};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00133};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC       ECO:0000256|HAMAP-Rule:MF_00133}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|ARBA:ARBA00009982,
CC       ECO:0000256|HAMAP-Rule:MF_00133}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXS50426.1}.
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DR   EMBL; LSBN01000003; KXS50426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139DA73; -.
DR   PATRIC; fig|1794808.3.peg.2164; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000070487; Unassembled WGS sequence.
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; 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   PIRSF; PIRSF001413; Trp_syn_beta; 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, ECO:0000256|HAMAP-
KW   Rule:MF_00133};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00133};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00133};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00133};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00133}.
FT   DOMAIN          51..375
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         85
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   394 AA;  43408 MW;  B4455EF7E8C366F8 CRC64;
     MSRGYFEEFG GRFVPETLMP ALDELEDVYL EMKEDPDFIN ELKSLLADYS GRPTSLYYAE
     QLTRHYGGAK IYLKREDLNH TGAHKINNTL GQILLAKKMG KKRIIAETGA GQHGVATATV
     AARFNLDCEI YMGAEDIERQ ALNVYKMEML GAEVIPVTSG TQTLKDATNE AIRDWVTNVE
     DTHYIIGSVV GPHPYPEMVR DFQRIIGDEA KKQIKEKEGR LPDYILACVG GGSNAMGIFY
     PFVEDQEVNL IGIEASGKGI ESGEHAATLS VGRVGVLHGS KSYLLQDDDG QVIPAYSISA
     GLDYPGVGPE HSYLKSIKRV DYQSATDLEA VAAFKLLSEK EGIIPALESS HALSYLEKLA
     PKLGEDQIIV VNLSGRGDKD INNFKKIREA EKDE
//
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