ID H5X1X4_9PSEU Unreviewed; 263 AA.
AC H5X1X4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=SacmaDRAFT_3840 {ECO:0000313|EMBL:EHR52043.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR52043.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR52043.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR52043.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
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; CM001439; EHR52043.1; -; Genomic_DNA.
DR RefSeq; WP_009155421.1; NZ_CM001439.1.
DR AlphaFoldDB; H5X1X4; -.
DR STRING; 882083.SacmaDRAFT_3840; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_11; -.
DR OrthoDB; 9804578at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000004926; 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 Reference proteome {ECO:0000313|Proteomes:UP000004926};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00131}.
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 263 AA; 27088 MW; A60EFAFEE482A276 CRC64;
MSRLGELFER TGQEGRAALV GYLPAGYPTV SRSKELLAAT IDAGTDLVEV GVPYSDPVMD
GPTIQAAADE ALRGGFRLRQ LFDVVESVAA RGGRAVVMTY YNPVFHYGVD AFARDLAAAG
GLGLITPDLT PDEAGEWLEA SQRHGLDRIF LVAPSSSEER IALTVKATTG FVYATAVMGV
TGARDSVGAG AAELVRRTRG HTDLPIGVGL GVRSGDQAAE VAGFADAVIV GSALVAKAAE
GTSAVSALTA ELAEGVRRPA VTA
//