TRPA_OCEIH
ID TRPA_OCEIH Reviewed; 262 AA.
AC Q8ESU5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; OrderedLocusNames=OB0521;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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DR EMBL; BA000028; BAC12477.1; -; Genomic_DNA.
DR RefSeq; WP_011064924.1; NC_004193.1.
DR AlphaFoldDB; Q8ESU5; -.
DR SMR; Q8ESU5; -.
DR STRING; 221109.22776200; -.
DR EnsemblBacteria; BAC12477; BAC12477; BAC12477.
DR KEGG; oih:OB0521; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_9; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 912786at2; -.
DR PhylomeDB; Q8ESU5; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000822; 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; -; 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 PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..262
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098818"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 262 AA; 28458 MW; 18DDC93227ACD2AE CRC64;
MGKSKLDAVL KEKTQAKKPI FVPYIMAGDG GIDNLNKRIQ FLEEAGASAV ELGIPFSDPV
ADGPVIQDAG QRALANKTTI GSVLEALESE KSQRNIPVVL MTYINPVWKY GFEQFARDCS
QAGVDGIIIP DIPMEEEDDV ASSLTQHDIA FIRLAAMTST EDRLERIAKR SEGFLYAVSV
TGTTGERAQH ENDAFHFLEK LKQISHVPVL AGFGISTAER ARELSAACDG VVVGSKIVQL
FEQGDEDGIH SLIRESIGEK VI