ID   Q17ZP4_HELAH            Unreviewed;       393 AA.
AC   Q17ZP4;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 118.
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:CAJ98882.1};
GN   OrderedLocusNames=Hac_0014 {ECO:0000313|EMBL:CAJ98882.1};
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638 {ECO:0000313|EMBL:CAJ98882.1, ECO:0000313|Proteomes:UP000000775};
RN   [1] {ECO:0000313|EMBL:CAJ98882.1, ECO:0000313|Proteomes:UP000000775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba {ECO:0000313|EMBL:CAJ98882.1,
RC   ECO:0000313|Proteomes:UP000000775};
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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, ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; AM260522; CAJ98882.1; -; Genomic_DNA.
DR   RefSeq; WP_011577004.1; NC_008229.1.
DR   AlphaFoldDB; Q17ZP4; -.
DR   STRING; 382638.Hac_0014; -.
DR   KEGG; hac:Hac_0014; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_7; -.
DR   OrthoDB; 9766131at2; -.
DR   BioCyc; HACI382638:HAC_RS00065-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000775; Chromosome.
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          52..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   393 AA;  42823 MW;  A7055F1D40481169 CRC64;
     MNKKAYFGEF GGSFVSELLV PALRELEQAF DACLKDDKFQ QEYFHLLKDF VGRPSPLTLC
     QNIISNPKVR LYLKREDLIH GGAHKTNQAL GQALLAKKMG KTRIIAETGA GQHGVATAIA
     CALLNLKCVI FMGGKDIKRQ EMNVFRMRLL GAEIREVNSG SATLKDAVNE TLRDWASSYK
     DTHYLLGTAA GPHPYPTMVK TFQKMIGDEA KQQILEKENR LPDYVIACVG GGSNAIGIFS
     AFLNDKEVKL IGVEPAGLGL ETNKHGATLN KGRVGILHGN KTYLLQDDEG QIIESHSISA
     GLDYPGVGPE HSFLKESGRA IYESASDIEA LEAFSLLCQK EGIIPALESS HALAYALKLA
     QKCTQESIIV VNLSGRGDKD LNTVYSALKG DLK
//