ID M1PAS0_9CORY Unreviewed; 485 AA.
AC M1PAS0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN ORFNames=A605_13925 {ECO:0000313|EMBL:AGF73781.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF73781.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF73781.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF73781.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(2012).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of
CC tryptophan biosynthetic pathway. The first reaction is catalyzed by the
CC isomerase, coded by the TrpF domain; the second reaction is catalyzed
CC by the synthase, coded by the TrpC domain.
CC {ECO:0000256|ARBA:ARBA00025592}.
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 -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family.
CC {ECO:0000256|ARBA:ARBA00009847}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family.
CC {ECO:0000256|ARBA:ARBA00007902}.
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DR EMBL; CP003697; AGF73781.1; -; Genomic_DNA.
DR RefSeq; WP_015402195.1; NZ_JIAJ01000005.1.
DR AlphaFoldDB; M1PAS0; -.
DR STRING; 1121362.A605_13925; -.
DR KEGG; chn:A605_13925; -.
DR PATRIC; fig|1121362.3.peg.2831; -.
DR eggNOG; COG0134; Bacteria.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_007713_3_0_11; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000011723; Chromosome.
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; IPR001468; Indole-3-GlycerolPSynthase_CS.
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.
DR PROSITE; PS00614; IGPS; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000313|EMBL:AGF73781.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AGF73781.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000011723};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00135}.
FT DOMAIN 9..262
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 267..472
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 485 AA; 51381 MW; 4DF7898307CB3841 CRC64;
MAHKLPTVLE GIVEGRRGHL AEIRARIAHV DVAALPTSER SLYTSLGGGE PGGGRGLNRF
IMECKSSSPS LGMIREHYEP GEIAKIYSRF AAGISVLCEP DRFGGDYDHL ATVASSTHLP
VLCKDFIVDE VQIHAARYYG ADAILLMLSV LDDEEYAALA AEAGRFGLDV LTEVIDEDEV
ERALRLDAKI IGVNHRNLHD LSIDLSRSGR LAELIPADRV VVSESGIRDN ETVRRLGGHS
NGFLVGSQLT SQPDIERAAR ELVHGTNKVC GLTTATAAQA ARSAGAVYGG LVFEEASPRD
VSRETATEII ANEPGLTYVA VSRRASGYAE LLLDGVGAVQ VHAPYQGSVD AELDLVQAVR
AEVPEGVEVW RAVSMTKEHG PAIAEALAAD GTVDRLVLDA GEGGTGTSFD WGVVPDVVKR
HSLLAGGLGP DNAADALAVG CAGLDLNSGV EYPATAGEWA GRKDAGAIRR VFSTVRTFSY
PESDL
//
