ID F4AWD3_DOKS4 Unreviewed; 253 AA.
AC F4AWD3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Krodi_1969 {ECO:0000313|EMBL:AEE19952.1};
OS Dokdonia sp. (strain 4H-3-7-5) (Krokinobacter sp. (strain 4H-3-7-5)).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia.
OX NCBI_TaxID=983548 {ECO:0000313|EMBL:AEE19952.1, ECO:0000313|Proteomes:UP000008290};
RN [1] {ECO:0000313|EMBL:AEE19952.1, ECO:0000313|Proteomes:UP000008290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4H-3-7-5 {ECO:0000313|EMBL:AEE19952.1,
RC ECO:0000313|Proteomes:UP000008290};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
RN [2] {ECO:0000313|Proteomes:UP000008290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4H-3-7-5 {ECO:0000313|Proteomes:UP000008290};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A.,
RA Antranikian F.I., Woyke T.;
RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4H-3-7-5;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A.,
RA Antranikian F.I., Woyke T.;
RT "Complete sequence of Krokinobacter sp. 4H-3-7-5.";
RL Submitted (FEB-2011) 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; CP002528; AEE19952.1; -; Genomic_DNA.
DR RefSeq; WP_013751459.1; NC_015496.1.
DR AlphaFoldDB; F4AWD3; -.
DR STRING; 983548.Krodi_1969; -.
DR KEGG; kdi:Krodi_1969; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_10; -.
DR OrthoDB; 9804578at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000008290; 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 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ SEQUENCE 253 AA; 27750 MW; 1D32B5F0C5F38202 CRC64;
MNRIKQKLQE DKKLLSLYFT AGYPAIDDTV SILTQLQESG VDMVEIGLPF SDPLADGPTI
QESSTAALHN GMTTEKLFSQ LDGIRETIHI PLIVMGYFNP MLQYGVEKFC KRCQEIGIDG
IIMPDLPLAE YEAEYKAIFE KYGLINVFLI TPQTSDARIQ QLDAASDGFI YMVSSASTTG
GTSGFSNTTS DYFERIAAMN LKSQQIVGFG ISNEETFKAA TTHQKGAIIG SAFIKHITKN
GANSVASFVE TIR
//
