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Database: UniProt
Entry: I1BYM5_RHIO9
LinkDB: I1BYM5_RHIO9
Original site: I1BYM5_RHIO9 
ID   I1BYM5_RHIO9            Unreviewed;       757 AA.
AC   I1BYM5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE            EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
DE   AltName: Full=Para-aminobenzoate synthase {ECO:0000256|ARBA:ARBA00031329};
DE   AltName: Full=p-aminobenzoic acid synthase {ECO:0000256|ARBA:ARBA00031904};
GN   ORFNames=RO3G_06010 {ECO:0000313|EMBL:EIE81305.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE81305.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE81305.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-
CC         glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85;
CC         Evidence={ECO:0000256|ARBA:ARBA00001000};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC       aminobenzoate from chorismate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005009}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC       synthase component I family. {ECO:0000256|ARBA:ARBA00005970}.
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DR   EMBL; CH476735; EIE81305.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1BYM5; -.
DR   STRING; 246409.I1BYM5; -.
DR   VEuPathDB; FungiDB:RO3G_06010; -.
DR   eggNOG; KOG0026; Eukaryota.
DR   eggNOG; KOG1224; Eukaryota.
DR   InParanoid; I1BYM5; -.
DR   OMA; TQWHPES; -.
DR   OrthoDB; 201921at2759; -.
DR   UniPathway; UPA00077; UER00149.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF18; AMINODEOXYCHORISMATE SYNTHASE; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 2.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..133
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          173..209
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          265..398
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          466..742
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   ACT_SITE        60
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   757 AA;  85957 MW;  B3CECD21825DD04C CRC64;
     MIFIRDEFVV DVLPYFDNII ISPGPGRPER QSDFGICTQL LQAQLDPNQS EYHRPIFGIC
     LGHQGIGHLL GGKVTYAPRI MHGRMSQVHI LPSKNDILTD CLSPFWAVRY HSLVVDKDSL
     PEDLILTGYC FENEADTEAL SNAHYIADHP PLSDTTSHRN HFLSHNVKDQ GTQQVTVMAF
     QHRSLPLWGV QFHPESVSTE HGEQMMLNFQ KETLRWLHQQ PVKTAPLSSR LLSYSAALPK
     THRIEQTHAF RAIVKTLDYW IDPGEVAERC NPVCWLDSSR TSSPYSRQSI LSTEPAFTLS
     YTTLQKQLTV TDRDQEWQET LSVTFFDYLA ELVGRIEKMP SDQFQGGFVG YFGYEMKRES
     LDGYHTPAEQ QYPHHGEPDA AFQFIDKFIV FDHTRHTISL TCLVQTKKEG NGSLLDKAGF
     HHEEQALAWM DHQTQLLFNH KPITIISTPP RSPKHQSTDL VPDVEHDHYL KNIDQCIQSI
     KEGDAYEICL TTRFRLNLPN INNFKELYTK HLRRNNPAPF SALVQFPSVC LMSSSPERFL
     SVSADHKSEM KPIKGTISRV LSCICEAGTC DQGSLCEERR QRGDEERKQQ LWQDVKERAE
     NLMIVDLIRN DLAQVCEPSS VHVPKLMHVE TYEKVHHLVS TIRGQLYPEV NSVKALQRCF
     PPGSMTGAPK LRAVQLLDEL EGHRPRGAYS GCLGYFSLNG SADFNVVIRT AVLINDELSV
     GGGGAITFLS DPEQEWKETL LKTKSVAPSV KEFLHSM
//
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