(data stored in SCRATCH zone)

SWISSPROT: A4AT95_MARSH

ID   A4AT95_MARSH            Unreviewed;       260 AA.
AC   A4AT95;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01103933};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01093371};
GN   Name=trpA {ECO:0000256|HAMAP-Rule:MF_00131};
GN   OrderedLocusNames=FB2170_16311 {ECO:0000313|EMBL:EAR00665.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00665.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00665.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
CC       of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00131,
CC       ECO:0000256|SAAS:SAAS01111173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine =
CC         D-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;
CC         EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00131,
CC         ECO:0000256|SAAS:SAAS01126077};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00131, ECO:0000256|SAAS:SAAS01093362}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_00131, ECO:0000256|SAAS:SAAS01111165}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00131, ECO:0000256|RuleBase:RU003662,
CC       ECO:0000256|SAAS:SAAS01111172}.
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DR   EMBL; CP002157; EAR00665.1; -; Genomic_DNA.
DR   RefSeq; WP_013304468.1; NC_014472.1.
DR   STRING; 313603.FB2170_16311; -.
DR   EnsemblBacteria; EAR00665; EAR00665; FB2170_16311.
DR   KEGG; fbc:FB2170_16311; -.
DR   eggNOG; ENOG4105F6H; Bacteria.
DR   eggNOG; COG0159; LUCA.
DR   HOGENOM; HOG000223816; -.
DR   KO; K01695; -.
DR   OMA; DYPPEEC; -.
DR   OrthoDB; 912786at2; -.
DR   BioCyc; MSP313603:G1GNS-41-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001602; 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; -; 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   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00262; trpA; 1.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AT95.
DR   SWISS-2DPAGE; A4AT95.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS01093358};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS01093369};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS01093361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00131,
KW   ECO:0000256|SAAS:SAAS01093372}.
FT   ACT_SITE     45     45       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
FT   ACT_SITE     56     56       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00131}.
SQ   SEQUENCE   260 AA;  29073 MW;  2236DC70E9B12122 CRC64;
     MNRINQRLLE DEKILSIYFT AGFPKIDDTV KIIEDLEKNG VDLIEIGLPF SDPLADGPTI
     QESSTIALNN GMHTELLFEQ IKDIRNTVSI PLIIMGYFNP IFQYGVEAFC KRCNEIGIDG
     LILPDLPLDV YQDEYATIFE KYGLVNVFLI TPQTSDERIK QIDEASNGFI YMVSSASTTG
     ATSGFGKEQQ EYFNRISSLN LKSPKIVGFG INNSETFRQA TRTTSGAIIG SAFIKHLRKH
     GTDSISKFLK NVRESHGDNQ
//

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