ID X2HZH7_HELPX Unreviewed; 262 AA.
AC X2HZH7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000256|HAMAP-Rule:MF_00131};
GN ORFNames=HPOKI112_06785 {ECO:0000313|EMBL:AHN36707.1};
OS Helicobacter pylori oki112.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1382921 {ECO:0000313|EMBL:AHN36707.1, ECO:0000313|Proteomes:UP000019647};
RN [1] {ECO:0000313|EMBL:AHN36707.1, ECO:0000313|Proteomes:UP000019647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oki112 {ECO:0000313|EMBL:AHN36707.1};
RX PubMed=24744331;
RA Satou K., Shiroma A., Teruya K., Shimoji M., Nakano K., Juan A.,
RA Tamotsu H., Terabayashi Y., Aoyama M., Teruya M., Suzuki R., Matsuda M.,
RA Sekine A., Kinjo N., Kinjo F., Yamaoka Y., Hirano T.;
RT "Complete Genome Sequences of Eight Helicobacter pylori Strains with
RT Different Virulence Factor Genotypes and Methylation Profiles, Isolated
RT from Patients with Diverse Gastrointestinal Diseases on Okinawa Island,
RT Japan, Determined Using PacBio Single-Molecule Real-Time Technology.";
RL Genome Announc. 2:e00286-14(2014).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000256|HAMAP-Rule:MF_00131}.
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_00131};
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_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00131, ECO:0000256|RuleBase:RU003662}.
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DR EMBL; CP006821; AHN36707.1; -; Genomic_DNA.
DR RefSeq; WP_025276345.1; NZ_CP006821.1.
DR AlphaFoldDB; X2HZH7; -.
DR KEGG; hpyc:HPOKI112_06785; -.
DR HOGENOM; CLU_016734_0_2_7; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000019647; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR NCBIfam; TIGR00262; trpA; 1.
DR PANTHER; PTHR43406:SF1; TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43406; TRYPTOPHAN SYNTHASE, ALPHA CHAIN; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00131};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00131};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00131};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 59
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 262 AA; 28807 MW; B1C02C6CB3AAEC1C CRC64;
MRYQNMFETL KKHEKMAFIP FVTLGDPNYE LSFEIVKTLI TSGVSALELG FAFSDPIADG
VTIQASHLRA LKHASMAKNF QLLKKIRGYN DDIPIGLLAY ANLIFSYGVD DFYAQIKECG
IDSVLIADMP LIEKELVIKS AQKHQIKQIF IASPNASSKD LEQVAMHSQG YIYTLARSGV
TGISHALEND ASTIIKTLKT FSPTPALLGF GISQKEHIKN AKEMGADGVI CGSALVKIIE
ENLNNENAML EKIKGFIGGM IF
//
