ID B2AXK8_PODAN Unreviewed; 756 AA.
AC B2AXK8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Multifunctional tryptophan biosynthesis protein {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=Anthranilate synthase component 2 {ECO:0000256|PIRNR:PIRNR001382};
DE Short=AS {ECO:0000256|PIRNR:PIRNR001382};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001382};
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|PIRNR:PIRNR001382};
DE Short=IGPS {ECO:0000256|PIRNR:PIRNR001382};
DE EC=4.1.1.48 {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|PIRNR:PIRNR001382};
DE Short=PRAI {ECO:0000256|PIRNR:PIRNR001382};
DE EC=5.3.1.24 {ECO:0000256|PIRNR:PIRNR001382};
GN ORFNames=PODANS_7_10910 {ECO:0000313|EMBL:CAP69132.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP69132.1};
RN [1] {ECO:0000313|EMBL:CAP69132.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP69132.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP69132.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP69132.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP32612.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase
CC (GATase) domain of anthranilate synthase, indole-glycerolphosphate
CC synthase, and phosphoribosylanthranilate isomerase activities.
CC {ECO:0000256|PIRNR:PIRNR001382}.
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 ECO:0000256|PIRNR:PIRNR001382};
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|PIRNR:PIRNR001382};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000256|PIRNR:PIRNR001382};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873,
CC ECO:0000256|PIRNR:PIRNR001382}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC ECO:0000256|PIRNR:PIRNR001382}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC ECO:0000256|PIRNR:PIRNR001382}.
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DR EMBL; CU633900; CAP69132.1; -; Genomic_DNA.
DR EMBL; FO904942; CDP32612.1; -; Genomic_DNA.
DR RefSeq; XP_001908459.1; XM_001908424.1.
DR AlphaFoldDB; B2AXK8; -.
DR STRING; 515849.B2AXK8; -.
DR MEROPS; C26.959; -.
DR GeneID; 6192053; -.
DR KEGG; pan:PODANSg5494; -.
DR VEuPathDB; FungiDB:PODANS_7_10910; -.
DR eggNOG; KOG0026; Eukaryota.
DR eggNOG; KOG4201; Eukaryota.
DR eggNOG; KOG4202; Eukaryota.
DR HOGENOM; CLU_007713_2_0_1; -.
DR OrthoDB; 294181at2759; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001197; Chromosome 7.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-UniRule.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR CDD; cd00331; IGPS; 1.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016302; Anthranilate_synth_II.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR PIRSF; PIRSF001382; TrpG-trpC-trpF; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001382};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001382};
KW Decarboxylase {ECO:0000256|PIRNR:PIRNR001382};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Isomerase {ECO:0000256|PIRNR:PIRNR001382};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001382};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR001382}.
FT DOMAIN 26..214
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 248..510
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 573..750
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 756 AA; 81803 MW; E463B5E8930F3EAE CRC64;
MPAIIDHSPH HPDPSPLVPT ASNLILIDNY DSFTWNVYQY LVLEGAKVTV FRNDQITLEE
LIAKKPTQLV ISPGPGHPGT DSGISRDAIK HFAGKVPIFG VCMGQQCMID LYGGEVSFAG
EILHGKTSPL CHDGKGVYAG LAQDLPVTRY HSLAGTHVTL PKCLQVTSWI ANQDGSKGVI
MGVRHTEYTI EGVQFHPESI LSADGRLMLK NFLYMQGGTW AENEQLQKAS QESKIVPKKA
TPAKNNILQK IYAHRKEAVA AQKQIPSQRP SDLQAAYNLN LAPPQISLVD RLRQSPFDVA
LAAEIKRGSP SKGIFALDID APTQARRYAL AGASVISVLT EPEWFKGSIE DLRAVRQVLN
GMPNRPAVLR KEFIFEEYQI LEARLAGADT VLLIVKMLET DLLERLYKYS LSLGMEPLVE
VQNAEEMTIA IKLGAKVIGV NNRNLENFEV DLGTTGRLKE MVPKDTFLLA LSGINSHQDV
LDCKRDGING ILVGEAIMRA PDASKFIREL CAGPEAAAPQ SVTNPMLVKI CGTRSAEAAT
EAIKAGADLV GMILVPGTKR CVSDETALAI SKAVHDAQTT AGEAVKLPKS ATDFFSVSAE
LLRKHRPLLV GVFMNQPLEE VLEKQRLYNL DIVQLHGDEP LEWASLIPVP VIRKFKPGQV
GVGVRGYHAV SLLDSGAGTG KLLDVESVKA ELEKDAELQV LLAGGLEPGN VTESVKALGA
LGGQVIGVDV SSGVEEDGKQ SLEKIRAFVK AAKAIR
//
