ID A0A0Q9YKR4_9COXI Unreviewed; 455 AA.
AC A0A0Q9YKR4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
GN Name=trpC {ECO:0000313|EMBL:KRG21309.1};
GN Synonyms=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN ORFNames=HT99x_01485 {ECO:0000313|EMBL:KRG21309.1};
OS Candidatus Berkiella aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG21309.1, ECO:0000313|Proteomes:UP000051497};
RN [1] {ECO:0000313|EMBL:KRG21309.1, ECO:0000313|Proteomes:UP000051497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT99 {ECO:0000313|EMBL:KRG21309.1,
RC ECO:0000313|Proteomes:UP000051497};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001633};
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|ARBA:ARBA00001164,
CC ECO:0000256|HAMAP-Rule:MF_00135};
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 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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:KRG21309.1}.
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DR EMBL; LKAJ01000005; KRG21309.1; -; Genomic_DNA.
DR RefSeq; WP_075066113.1; NZ_LKAJ02000001.1.
DR AlphaFoldDB; A0A0Q9YKR4; -.
DR STRING; 295108.HT99x_01485; -.
DR PATRIC; fig|1590043.3.peg.1515; -.
DR OrthoDB; 9804217at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000051497; Unassembled WGS sequence.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00331; IGPS; 1.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000051497};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00135}.
FT DOMAIN 2..249
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 255..449
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 455 AA; 50580 MW; 046794134DC18608 CRC64;
MLNEMIKDQH ALVADLMKQQ SETALLKAVI PSDRDFYAAL QKSGSKFILE CKHRSPSEGR
LREDYPIIEL AKTYEPFADI ISVLTNERHF DGSFTHLQQV RQHVNVPVLC KDIIVAPYQV
ALARQYGADA ILLMLSVLDD TTYLACQQLA EKLKMGILTE VVNPQELQRA KKLKAKVIAI
NHRDLHTLTL DMERVVSLAP LFPKETIMIA ASGLNTHQDI ARLKPYVKGF LIGGALSKSQ
DIAITLRELR YGAIKICGLT SSIDSQYSYE HGAILGGLIF AASSPRTINL AQAEEIIKGA
PLQYVGVFAK QPIHDVIHIA TTLKLHAIQL HGQETADYIA KLRPLLPKSC QIWFAVSGHQ
PLPLTLPPHI DKLIIDNMAP TQLGGTGRSF DWNKLRHFHL RQHCLLAGGV GLHNIIAATQ
TKLAGLDINS SIEQTPGIKD HLKIKQLFQM IRENT
//
