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Database: UniProt
Entry: A0A0F7KNW6_9SPHN
LinkDB: A0A0F7KNW6_9SPHN
Original site: A0A0F7KNW6_9SPHN 
ID   A0A0F7KNW6_9SPHN        Unreviewed;       263 AA.
AC   A0A0F7KNW6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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   ECO:0000313|EMBL:AKH41254.1};
GN   ORFNames=FHS61_001781 {ECO:0000313|EMBL:MBB5732772.1}, WYH_00189
GN   {ECO:0000313|EMBL:AKH41254.1};
OS   Croceibacterium atlanticum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH41254.1, ECO:0000313|Proteomes:UP000034392};
RN   [1] {ECO:0000313|EMBL:AKH41254.1, ECO:0000313|Proteomes:UP000034392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=26DY36 {ECO:0000313|EMBL:AKH41254.1,
RC   ECO:0000313|Proteomes:UP000034392};
RA   Wu Y.-H., Cheng H., Wu X.-W.;
RT   "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5732772.1, ECO:0000313|Proteomes:UP000556014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100738 {ECO:0000313|EMBL:MBB5732772.1,
RC   ECO:0000313|Proteomes:UP000556014};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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; CP011452; AKH41254.1; -; Genomic_DNA.
DR   EMBL; JACIJL010000003; MBB5732772.1; -; Genomic_DNA.
DR   RefSeq; WP_046902331.1; NZ_CP011452.2.
DR   AlphaFoldDB; A0A0F7KNW6; -.
DR   STRING; 1267766.WYH_00189; -.
DR   KEGG; aay:WYH_00189; -.
DR   PATRIC; fig|1267766.3.peg.193; -.
DR   OrthoDB; 9804578at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000034392; Chromosome.
DR   Proteomes; UP000556014; 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   Reference proteome {ECO:0000313|Proteomes:UP000034392};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00131}.
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT   ACT_SITE        53
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   263 AA;  27192 MW;  6194BB2946DB9908 CRC64;
     MSRLSNAFAK GHPALLCFLT AGDGDTAANL DALVEGGADV IELGMPFTDP MADGPAIQAA
     NLRSLGKGTT TRDVLMIANE FRERHPDVPL VLMGYANPMV RRGPEWFAGE AKGCGVDGVI
     CVDLAPEEDP DLGPALRAAG VDFIRLATPT TDDARLPAVL DGSGGFLYYV SVAGITGQQQ
     AALDSIEQAV ARLKKATDLP VAVGFGVRTP EQAAAIARVA EGVVVGSALV ELVGEHGEDA
     PARLRELTAS LAKAVHSARE GAL
//
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