ID U0EH64_9NOCA Unreviewed; 267 AA.
AC U0EH64;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=N806_14920 {ECO:0000313|EMBL:ERB52461.1};
OS Rhodococcus sp. P27.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1384060 {ECO:0000313|EMBL:ERB52461.1, ECO:0000313|Proteomes:UP000016008};
RN [1] {ECO:0000313|EMBL:ERB52461.1, ECO:0000313|Proteomes:UP000016008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P27 {ECO:0000313|EMBL:ERB52461.1,
RC ECO:0000313|Proteomes:UP000016008};
RX PubMed=24072865;
RA Gouvea Taketani R., Domingues Zucchi T., Soares de Melo I., Mendes R.;
RT "Whole-Genome Shotgun Sequencing of Rhodococcus erythropolis Strain P27, a
RT Highly Radiation-Resistant Actinomycete from Antarctica.";
RL Genome Announc. 1:e00763-13(2013).
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}.
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:ERB52461.1}.
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DR EMBL; AVCO01000032; ERB52461.1; -; Genomic_DNA.
DR AlphaFoldDB; U0EH64; -.
DR PATRIC; fig|1384060.5.peg.3736; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000016008; Unassembled WGS sequence.
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 53
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 267 AA; 27644 MW; 8F2A3E44923520BE CRC64;
MSERPSRLAP TFAACKADKR AALVGYLPAG YPTVPESIDV FKAMVDGGCD IIEVGVAYSD
PVMDGPTIQR AAETALTNGV RLSDIFTVIE QISSVGGKAV VMTYWNPVLQ YGVDKFARDL
ASAGGLGLIT PNLIPEEAGA WMEASEEHHL DRIFLVAPSS TEERLAMTLD ASSGFIYAAS
TMGVTGARDA VSSMAPELTA RIRAHSDIPV GVGLGVRSGA QAAEIAAYAD AVIVGSALVS
AVENGLGAVR SLTEELAKGV RSATVAS
//