ID   H1AFK5_SHEFR            Unreviewed;       267 AA.
AC   H1AFK5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
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:BAL45195.1};
OS   Shewanella frigidimarina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=56812 {ECO:0000313|EMBL:BAL45195.1};
RN   [1] {ECO:0000313|EMBL:BAL45195.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K14-2 {ECO:0000313|EMBL:BAL45195.1};
RA   Ishdia M., Mita M.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAL45195.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K14-2 {ECO:0000313|EMBL:BAL45195.1};
RA   Mitsuya D., Tanaka S., Matsumura H., Urano N., Takano K., Ogasahara K.,
RA   Yutani K., Ishida M.;
RT   "The crystal strucutre of the tryptophan synthase alpha subunit from the
RT   psychrophile Shewanella frigidimarina.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007829|PDB:3VND}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RX   PubMed=24163283; DOI=10.1093/jb/mvt098;
RA   Mitsuya D., Tanaka S., Matsumura H., Urano N., Takano K., Ogasahara K.,
RA   Takehira M., Yutani K., Ishida M.;
RT   "Strategy for cold adaptation of the tryptophan synthase alpha subunit from
RT   the psychrophile Shewanella frigidimarina K14-2: crystal structure and
RT   physicochemical properties.";
RL   J. Biochem. 155:73-82(2014).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB690266; BAL45195.1; -; Genomic_DNA.
DR   PDB; 3VND; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-267.
DR   PDBsum; 3VND; -.
DR   AlphaFoldDB; H1AFK5; -.
DR   SMR; H1AFK5; -.
DR   UniPathway; UPA00035; UER00044.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3VND};
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        50
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   267 AA;  27806 MW;  FC55FDE6C55A3E40 CRC64;
     MSNRYQAKFA ALKAQDKGAF VPFVTIGDPS PELSLKIIQT LVDNGADALE LGFPFSDPLA
     DGPVIQGANL RSLAAGTTSS DCFDIITKVR AQHPDMPIGL LLYANLVFAN GIDEFYTKAQ
     AAGVDSVLIA DVPVEESAPF SKAAKAHGIA PIFIAPPNAD ADTLKMVSEQ GEGYTYLLSR
     AGVTGTESKA GEPIENILTQ LAEFNAPPPL LGFGIAEPEQ VRAAIKAGAA GAISGSAVVK
     IIEAHQHDEA TLLAKLAEFT TAMKAAT
//