ID C1N8W1_MICPC Unreviewed; 863 AA.
AC C1N8W1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=MICPUCDRAFT_23429 {ECO:0000313|EMBL:EEH51423.1};
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN [1] {ECO:0000313|EMBL:EEH51423.1, ECO:0000313|Proteomes:UP000001876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH51423.1,
RC ECO:0000313|Proteomes:UP000001876};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(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; GG663751; EEH51423.1; -; Genomic_DNA.
DR RefSeq; XP_003064518.1; XM_003064472.1.
DR AlphaFoldDB; C1N8W1; -.
DR STRING; 564608.C1N8W1; -.
DR MEROPS; C26.955; -.
DR GeneID; 9689783; -.
DR KEGG; mpp:MICPUCDRAFT_23429; -.
DR eggNOG; KOG1224; Eukaryota.
DR OMA; DWSVNIR; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000001876; 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 NCBIfam; TIGR00566; trpG_papA; 1.
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; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
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|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000001876};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 127..320
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 441..493
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 540..842
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 863 AA; 90226 MW; 32BB7844DE5DE7DB CRC64;
MSSAAASGAP PTAAIGADDA NNPTTKNAAT VVDVDESPPL FATASSFPGA DDASLNDEEW
LSRALAAAAT TTATTTASSS STNDPRRASD PAPSSSDPAP RATAAATAPS YPPRALATTT
WHGDRTLLID NHDSYTYNLY HLIAAADGVP PVVLRNDSVT WPELEPSISS RHFARVVLSP
GPGTPDVAGD VGVCMDLLLH AAETPILGVC LGHQARSALA AAHGGAVVRA PKPTHGRAHA
LRHDGDDMWR GIPSGGGGLV GVRYHSLVVD PGTLPECLTA TAPPVVIMGM RHKTRPHYGV
QYHPESVCST HGDALYRNFA AAADAHWKRG ALWRRAIYRC PPPPPPSDEN GPTADRAFRT
GAAPAFAGGS LTVTDATGAS TTRTGVSVLE WLESRLRSRR CRRAEEVTLN VKRSREDETS
TDEPAIDDAD FIADGRLPNL PFDFIGGFVG YLGYEIRRCG CHPPSRASPT PDAALFLADR
VVAIDHDTDD VYLLAIVSDA ASELESLAEG MELHGAANAA ATGLCQLAAE EAEAEARANR
EAYVADVDAA KALIDAGETY EVCLTNELRR GGGGDGDDRP CPDPATLYAV LRRTNPAPYA
AYLNFGGCGG DGARGLDDAV VVCCSSPERF LRLTKKRGGR GGGDANDDAT VDAKPIKGTA
PRRHPLNGED DVREARELAS SVKDRAENLM IVDLLRNDLG RVCVPGSVSV PGLMKIESYA
TVHQARRSIT LLVSTVVGTR DEAAASPVAC ARAAFPPGSM TGAPKPRTME IIDALEPSAR
GAYSGSIGFF SVNDAFDLNV VIRTAVLKPG SKPGSGEVFI GAGGAITTLS DSSAEWEEAM
LKSRAIVRAV EACDELAARG AAP
//
