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Database: UniProt
Entry: A0A098S2P0_9BACT
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ID   A0A098S2P0_9BACT        Unreviewed;       398 AA.
AC   A0A098S2P0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=IX84_23375 {ECO:0000313|EMBL:KGE86083.1};
OS   Phaeodactylibacter xiamenensis.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC   Phaeodactylibacter.
OX   NCBI_TaxID=1524460 {ECO:0000313|EMBL:KGE86083.1, ECO:0000313|Proteomes:UP000029736};
RN   [1] {ECO:0000313|EMBL:KGE86083.1, ECO:0000313|Proteomes:UP000029736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD52 {ECO:0000313|EMBL:KGE86083.1,
RC   ECO:0000313|Proteomes:UP000029736};
RX   PubMed=25052393; DOI=10.1099/ijs.0.063909-0;
RA   Chen Z.Jr., Lei X., Lai Q., Li Y., Zhang B., Zhang J., Zhang H., Yang L.,
RA   Zheng W., Tian Y., Yu Z., Xu H.Jr., Zheng T.;
RT   "Phaeodactylibacter xiamenensis gen. nov., sp. nov., a member of the family
RT   Saprospiraceae isolated from the marine alga Phaeodactylum tricornutum.";
RL   Int. J. Syst. Evol. Microbiol. 64:3496-3502(2014).
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:KGE86083.1}.
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DR   EMBL; JPOS01000082; KGE86083.1; -; Genomic_DNA.
DR   RefSeq; WP_044226112.1; NZ_JPOS01000082.1.
DR   AlphaFoldDB; A0A098S2P0; -.
DR   STRING; 1524460.IX84_23375; -.
DR   OrthoDB; 9766131at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000029736; 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:UP000029736};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00133}.
FT   DOMAIN          55..377
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         88
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   398 AA;  43736 MW;  85A7F8015474ED25 CRC64;
     MIAVDERGYY GEFGGAYIPE MLYPNIEELR QRYLEIMQEE TFQKQFHRLL RDYVGRPSPL
     YLAERLSEHY NTNIYLKRED LNHTGAHKIN NTIGQILLAK RLGKKRIIAE TGAGQHGVAT
     ATVCALMGMP CVVYMGAVDI KRQAPNVSRM RMLGAEVRPA ESGSRTLKDA TNEAIRDWIN
     NPVDTHYIIG SAVGPHPYPD MVARFQSVIS EEMQWQLEEH TGRAKPDAVI ACVGGGSNAA
     GAYFHYLNEP DVRLIAVEAA GKGVHSGESA ATSILGTKGI IHGSRTLLMQ TKDGQIVEPY
     SLSAGLDYPG IGPMHAHLIA SGRAEAISIT DEEALKAAYF LSRKEGIIPA LETSHAFAAL
     DVMEYNSSDV IVICLSGRGD KDLETFINHF DDYQNGAL
//
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