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Database: UniProt
Entry: A0A365U7A5_9RHOB
LinkDB: A0A365U7A5_9RHOB
Original site: A0A365U7A5_9RHOB 
ID   A0A365U7A5_9RHOB        Unreviewed;       408 AA.
AC   A0A365U7A5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ECO:0000313|EMBL:RBI84303.1};
GN   ORFNames=DRV85_12735 {ECO:0000313|EMBL:RBI84303.1};
OS   Rhodosalinus halophilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodosalinus.
OX   NCBI_TaxID=2259333 {ECO:0000313|EMBL:RBI84303.1, ECO:0000313|Proteomes:UP000253370};
RN   [1] {ECO:0000313|EMBL:RBI84303.1, ECO:0000313|Proteomes:UP000253370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E84 {ECO:0000313|EMBL:RBI84303.1,
RC   ECO:0000313|Proteomes:UP000253370};
RA   Liu Z.-W., Lu D.-C.;
RT   "Rhodosalinus sp. strain E84T genomic sequence and assembly.";
RL   Submitted (JUL-2018) 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:RBI84303.1}.
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DR   EMBL; QNTQ01000011; RBI84303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365U7A5; -.
DR   OrthoDB; 9766131at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000253370; 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}; Reference proteome {ECO:0000313|Proteomes:UP000253370};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00133}.
FT   DOMAIN          64..389
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         98
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   408 AA;  44422 MW;  8D1DFBB4BDC265D7 CRC64;
     MPEDRINSFR SGPDAQGRFG DFGGRFVSET LMPLILELEA EYERAKTDAD FWAEMDDLWT
     HYVGRPSPLY FAERLTKHLG GAKVYMKRDE LNHTGAHKIN NVLGQILLAR RMGKTRIIAE
     TGAGQHGVAT ATVCAKFGLK CIVYMGAHDV ERQAPNVFRM KLLGAEVVPV TSGRGTLKDA
     MNDALRDWVT NVRDTFYCIG TVAGPHPYPA MVRDFQSIIG QEVRRQMTEA EGRLPDTLVA
     AIGGGSNAMG LFHPFLDDPE VAIVGVEAGG RGVNEKMEHC ASLTGGRPGV LHGNRTYLLQ
     DDDGQILEGY SISAGLDYPG IGPEHAWLHE SGRAQYVSVT DDEALDAFKL CCEMEGIIPA
     LEPSHALAHV TKVAPDLPSD HIICMNMCGR GDKDIFTVAR ALGVDISG
//
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