ID A0A196SFL2_BLAHN Unreviewed; 1368 AA.
AC A0A196SFL2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:OAO14937.1};
GN ORFNames=AV274_3363 {ECO:0000313|EMBL:OAO14937.1};
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO14937.1, ECO:0000313|Proteomes:UP000078348};
RN [1] {ECO:0000313|EMBL:OAO14937.1, ECO:0000313|Proteomes:UP000078348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAO14937.1}.
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DR EMBL; LXWW01000195; OAO14937.1; -; Genomic_DNA.
DR STRING; 478820.A0A196SFL2; -.
DR OrthoDB; 101575at2759; -.
DR Proteomes; UP000078348; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000078348}.
FT DOMAIN 44..157
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 183..231
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 525..662
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 907..1032
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 468..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1198
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1368 AA; 152489 MW; 2E7C8AD93D771F57 CRC64;
MLTCSNQLVH YYRYPGLTCA TEENILRKLQ NALGNCVKEI KTELCYNLDV SCDFKEEEKD
VVRFLLSESY NQNGFGTHSF LKKEGPYDLL VEVGPRINIV TAWCTNALSI FRSSNITNVR
RIEMSKRYLI VSDEALCLKT VESLLHDEMT ETIYTETLQS FAANNTPEEV QTIPVMEEGE
TAIERINLAW SLALSPDEVR LITSIFRDKL HRNPTDVELM DLFQSNNEHC RRYLCNGKVV
VDGEEKPFTM NQLLQACKPV TAFPSTMISF GKDGSAIKGT LAEALNSETP YEPSRTISTF
QNKNPVVTMT THNFPSGVTP FPGAETGVGG QIREVVSTGN GAKVIGGASG LFVGNLNIPG
YHQPWEEASD YPKLYSSPLT ILLEASAGAA DYANKFGEPI IAGTTRSFGS VLPSGERSEY
IKPVVISDGF GICYDSIHTD EAIDDDIVIA KIGGPAFRMG LKGGVYSSKQ QETNHRKKHH
STNSSMSRRS VDRALGTASE SPRQEEDALH VGESASQEES VSPRQEEEEA AEPNIDFEGV
QRGDAEMGNK LCRVINTCVT MGQKNPILHI FNQGAGGNSH IMKMIVECRS KEKSGVMVDL
DRIVLGDKSL SAREIWGAEY QENVCVLIKK ENIELLRKIC ERERIYFMVI GKVTNSGKIE
VFSNRQLVVD LPVDLTYTNI PQHVYTDTSR PLVTRPLVLP STFSLTDLVT RTFHLLSVGS
KRFFVNKFDR SITGLIASQP CCGPLFLPIA DVAVIAKDYR SRTSGLAYAI GEQPIKSFIS
ARNMVRLTIG EAMTNLVFGN VNSYSDIHFV LSFNCAGKLP GETAYMYQCC EEIQQCMKEL
RLEIVNVKDS VSMAVCMGEQ TVKAPFTLVA TAFANCEEVL DIVTPDVKHA AQRSKLLFID
LNDSAPSLGG SALAQVFDQV GDSCPSVDLA LLQRAFRILH SLIKQQHVLA GHDRSDGGLI
TTLLEMVFAG DCGAEITLPE GVDSTAYLFN EGLGWVIEVD EPLCEPLLRS FADSSVSAVV
VGTTTTERRV VVKQGERVLL DEATLALREE WERTSYELEL MTYNKTYVEK EHEARKTMRA
PQWHATFLPS PTKNALLLNS NKYRVGIVRE EGTNCDREMV AAFFKSGLEP WLITISDLMD
RRANVRDFSG LVFCGGFSFG DVLDSARGWA GCILFNKTIK DQFEWYAKQE DRFTLGVCNG
CQLMSQINYV PFPLPDRAKQ PRFIQNRAGK LECRVVNVRI EKSKSVLLRG MEGSTLGVWI
AHGEGRCYWP DAAVKAEAER QGCVAMKYVD NEGNYAEDYP YNPNGSDSSI AALCSADGRH
LCMMPHPERT LTRWAWPYWP EEWDFTESPW LKLFQNARLW CEEVHRQD
//
