ID   A0KVD2_SHESA            Unreviewed;       493 AA.
AC   A0KVD2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00134, ECO:0000256|HAMAP-Rule:MF_00135};
DE   Includes:
DE     RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00134};
DE              Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE              EC=4.1.1.48 {ECO:0000256|HAMAP-Rule:MF_00134};
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};
GN   Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN   Synonyms=trpC {ECO:0000256|HAMAP-Rule:MF_00134};
GN   OrderedLocusNames=Shewana3_1517 {ECO:0000313|EMBL:ABK47751.1};
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK47751.1, ECO:0000313|Proteomes:UP000002589};
RN   [1] {ECO:0000313|Proteomes:UP000002589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00134};
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       ECO:0000256|HAMAP-Rule:MF_00134}.
CC   -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00134}.
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; CP000469; ABK47751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0KVD2; -.
DR   STRING; 94122.Shewana3_1517; -.
DR   KEGG; shn:Shewana3_1517; -.
DR   eggNOG; COG0134; Bacteria.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_007713_1_0_6; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000002589; Chromosome.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
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_00134_B; IGPS_B; 1.
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_00134};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00134};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00134};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000313|EMBL:ABK47751.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00134};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00134}.
FT   DOMAIN          35..280
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
FT   DOMAIN          285..489
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  53347 MW;  70EEF2789494009F CRC64;
     MTQVQQPDAH RSEDNQASQD VRGSMQTSTA KANVLTRIVD TKAAHIAALK LRFPEDSLTP
     KISDRSLFAA LKAPKAGYIL ECKKASPSKG LIRKDFDVEA IASIYTQYAA GISVLTDEQF
     FQGDIDYIPK VRAKVSQPIL CKDFFVDEYQ VKLAAHQGAD AILLMLSVLE DERYQQLASE
     AAKYQLDVLT EVSNEEELKR AIALNAPIIG INNRNLRDLS TDLATTEALA PHIGSDRVVI
     SESGIYTNEQ VRRLSPLVDG FLVGSSIMAE EDIDLACRKL IFGHNKVCGL TRLEDIQAAA
     TAGAVYAGLI FAEKSPRALT QEAAKQLVQQ YRAANLPAIE FVGVFVNSTP ELMASVAQEC
     SLAALQLHGS ETELEIAELS QLLQQAGLNT QIWKAVSVDA QSGELAAMPR GVQRYLFDSK
     NDAGFGGTGQ AFNWQLPIAH KAEAMLAGGL NADNAARANA QGFYGLDFNS GLETAPGVKS
     AEKIQAAFSQ LRL
//