ID E7RK05_9BACL Unreviewed; 598 AA.
AC E7RK05;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|HAMAP-Rule:MF_00135};
DE Includes:
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000256|HAMAP-Rule:MF_00135};
DE Includes:
DE RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN Synonyms=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN ORFNames=GPDM_14126 {ECO:0000313|EMBL:EGA88611.1};
OS Planococcus donghaensis MPA1U2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA88611.1, ECO:0000313|Proteomes:UP000003052};
RN [1] {ECO:0000313|EMBL:EGA88611.1, ECO:0000313|Proteomes:UP000003052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA88611.1,
RC ECO:0000313|Proteomes:UP000003052};
RX PubMed=21994932; DOI=10.1128/JB.05983-11;
RA Pearson M.D., Noller H.F.;
RT "The Draft Genome of Planococcus donghaensis MPA1U2 Reveals Nonsporulation
RT Pathways Controlled by a Conserved Spo0A Regulon.";
RL J. Bacteriol. 193:6106-6106(2011).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133}.
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_00133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00135};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00133};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC ECO:0000256|HAMAP-Rule:MF_00135}.
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_00133}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|ARBA:ARBA00009982,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|HAMAP-
CC Rule:MF_00135}.
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:EGA88611.1}.
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DR EMBL; AEPB01000053; EGA88611.1; -; Genomic_DNA.
DR AlphaFoldDB; E7RK05; -.
DR eggNOG; COG0133; Bacteria.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000003052; Unassembled WGS sequence.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd00405; PRAI; 1.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00135; PRAI; 1.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00263; trpB; 1.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00135};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00135};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00133};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00133};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00135}.
FT DOMAIN 4..195
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT DOMAIN 258..580
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 598 AA; 64986 MW; E9F86C480410C836 CRC64;
MTKVKICGLK EEQHVQAASR ADAIGFVFAP SKRQVTIEQA AELAKHVPID AEKIGVFVNA
TLKEIEETVA GVPLTMVQLH GDESDELVRA IRVPVIQAFS IRTKEDVVKL KQSLADYVLV
DAPGTDYRGG SGNVFDWSLL EGADIDPARL IVAGGLNPGN VHAAIEQTTP YMVDVSSGVE
TDNRKDTVKI QEFIKSVKGD FVEETMEKVG FFGKYGGQFV PETLMKAVKE LEDAYNEVKE
DPEFHKEYHH YLSEYVGREQ PLTYAQRMTE AYGGPKIYLK REDLNHTGAH KVNNAIGQAL
LAMRMGKRKI VAETGAGQHG VATATICALF DLDCVIFMGE EDIKRQQLNV FRMKLLGARV
ESVTKGSATL KDAVNEALRY WVANVEDTHY LIGSALGPHP FPTMVRDFQS VIGEETKRQI
LAKEGRLPDA ILACIGGGSN AIGMFYPFIQ DKEVELIGVE AAGQGVDTAK HAATLTKGTD
GVLHGALMKL LQDDAGQVQE AHSISAGLDY PGIGPEHAHL ADTGRVEYRS ITDDEALAAV
ISMSRLEGII PALESAHAIA EAEKQAKQMT ADQILVICVS GRGDKDMATY AEKLEGLA
//
