ADCS_SCHPO
ID ADCS_SCHPO Reviewed; 718 AA.
AC O94277;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Putative aminodeoxychorismate synthase;
DE Short=ADC synthase;
DE EC=2.6.1.85;
DE AltName: Full=P-aminobenzoic acid synthase;
DE Short=PABA synthase;
DE AltName: Full=Para-aminobenzoate synthase;
GN ORFNames=SPBP8B7.29;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC)
CC from chorismate and glutamine. Required for the synthesis of 4-
CC aminobenzoate (PABA), an important component in tetrahydrofolate
CC biosynthesis (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21814.1; -; Genomic_DNA.
DR PIR; T40823; T40823.
DR RefSeq; NP_596536.1; NM_001022457.2.
DR AlphaFoldDB; O94277; -.
DR SMR; O94277; -.
DR BioGRID; 277893; 1.
DR STRING; 4896.SPBP8B7.29.1; -.
DR MEROPS; C26.A26; -.
DR iPTMnet; O94277; -.
DR MaxQB; O94277; -.
DR PaxDb; O94277; -.
DR PRIDE; O94277; -.
DR EnsemblFungi; SPBP8B7.29.1; SPBP8B7.29.1:pep; SPBP8B7.29.
DR GeneID; 2541382; -.
DR KEGG; spo:SPBP8B7.29; -.
DR PomBase; SPBP8B7.29; -.
DR VEuPathDB; FungiDB:SPBP8B7.29; -.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_0_1; -.
DR InParanoid; O94277; -.
DR OMA; DWSVNIR; -.
DR PhylomeDB; O94277; -.
DR UniPathway; UPA00077; UER00149.
DR PRO; PR:O94277; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; ISO:PomBase.
DR GO; GO:0046656; P:folic acid biosynthetic process; ISO:PomBase.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008153; P:para-aminobenzoic acid biosynthetic process; IBA:GO_Central.
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; -; 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; IPR010117; PabB_fungal.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR01823; PabB-fungal; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Folate biosynthesis; Glutamine amidotransferase;
KW Multifunctional enzyme; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..718
FT /note="Putative aminodeoxychorismate synthase"
FT /id="PRO_0000310363"
FT DOMAIN 9..203
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 266..718
FT /note="PABB component"
FT /evidence="ECO:0000250"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 718 AA; 80598 MW; 933AE5EF1F1D3820 CRC64;
MSEISNRLQI LLIDCYDSYT FNLYDLLYKA SENACVIVVH WDKMSPDLWE DILQFDAIVV
GPGPGHPAEY SSILNRIWQL NIPVMGICLG FQSLALYHGA TIERMPNLPW HGRVSSVTTS
KTFIFDGISA VKGMRYHSLY ANKIPIDSLQ ILAQSDEDNI VMSIKATKFP HFGILYHPES
VGSSKSLKIF KNFLSLADTP NIQCVNSFSK SANGFSHNLN RYDISPAAFI LKSGSPSLQI
HSVEIPWVEP LALADCIQKS GNPICFLDSA KKPGRYSILG ILTGPLARII HYEKATNTTE
IRICKDNSFV RINNDLWSTV ADFMNQHKAI KPDTNLPFYG GIMGIIGYEC SDLSTKSVSN
ASFPLDFQQT TVDAELAFVD RSFVFDLEIK KLFVQTLTPL NETCSEWWGE LLASTCNTKL
DNLSCLHSFD GKQNFGLVQS FPKKEVYCES VKACQEHLLA GDSYEMCLTD TTFVSAPPEL
SDFEMYMRAR SLNPATFAGF VRLNHFTLLC CSPERFLQFR DDRCLFSPIK GTLKREGHMS
LEEARKKLLN EKDMGELNMI IDLIRNDLHQ LAKKNSVHVP ELYSVEEHSN VYSLLSNIYG
RIESPITAWD VLSKSFPPGS MTGAPKLRSV RMLEPLEQHG RGIYSGTLGY WDVTGSAEFN
VIIRSAFKYK ADDYWRIGAG GAVTILSSPE GEYEEMVLKA NSILPAFVNL KNKKRSCK
