ID R9P810_PSEHS Unreviewed; 703 AA.
AC R9P810;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00033770};
DE EC=2.4.2.14 {ECO:0000256|ARBA:ARBA00011941};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|ARBA:ARBA00033776};
GN ORFNames=PHSY_001801 {ECO:0000313|EMBL:GAC94230.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC94230.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005209}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138}.
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DR EMBL; DF238783; GAC94230.1; -; Genomic_DNA.
DR RefSeq; XP_012187817.1; XM_012332427.1.
DR AlphaFoldDB; R9P810; -.
DR STRING; 1305764.R9P810; -.
DR GeneID; 24107096; -.
DR eggNOG; KOG0572; Eukaryota.
DR HOGENOM; CLU_022389_3_3_1; -.
DR OrthoDB; 4975at2759; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR NCBIfam; TIGR01134; purF; 1.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 106..351
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 653..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 76726 MW; 78FD51BD8A1E045D CRC64;
MRFGPFSRKR CDRGLSCNKT KTCAPACTAE STLLPAPCEA HSLVGQLVTG FVSDQPLPLA
SSPLGIHLTV LECRIVPRST VHLLTPTHLR FCFVIVVADV ASSTMCGITA LLLASTEQSA
APEINEALSL LQHRGQDAAG IVTCGSKGRF YQCKANGMVR DVFDVNAISR LQGSMGVGHV
RYPTAGSSAH SEAQPFYVNA PYGITFAHNG NLINTDELRR FLDADAHRHI NTDSDSEVLL
NVFANNLQKT GKFRINEEDI FTAIRDLMKQ CKGGYTCAAM IAGFGIIAFR DPNGIRPLGM
CSRPSSVADS EYLEGHGMDY LFTSESVVCD ALGFEDFQDI KPGEAVIITR HAVSRRILTP
PAGSQDGAAF SPDIFEYVYF ARPDSVMDGV SVYRSRMAMG DKLADEVRRQ LQKTGETIDV
VIPVPDTSRV AALQLAQNLG VPYREGFIKN RYVGRTFIMP GQSVRRKNVR RKLNAMALEF
NGKNVLIVDD SIVRGTTSKE IIQMARDAGA RKVIMASCAP PIRYSNVYGI DMPSRKELVA
YERSVEQVAE YIQADMVIYQ TLEDLIDSVQ QFNPELKQFD CSVFDGKYVT GGVDAAYIAH
LEHLRSENAK AKKAAGKIPV IAESQKKIYA SRASPAASSV AGDEKMANEA TAAVLNGNAN
GNRKRRLTDE EIEEEEEEKQ QAAGCSGPMN GADDIGLFNG WTR
//