PUR1_MYCTU
ID PUR1_MYCTU Reviewed; 527 AA.
AC P9WHQ7; L0T4Y9; O06626; P65829;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Flags: Precursor;
GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; OrderedLocusNames=Rv0808;
GN ORFNames=MTCY07H7A.01c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-
CC Rule:MF_01931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01931};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01931};
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:0000255|HAMAP-Rule:MF_01931}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931}.
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DR EMBL; AL123456; CCP43556.1; -; Genomic_DNA.
DR PIR; A70537; A70537.
DR RefSeq; NP_215323.1; NC_000962.3.
DR RefSeq; WP_003404129.1; NC_000962.3.
DR AlphaFoldDB; P9WHQ7; -.
DR SMR; P9WHQ7; -.
DR STRING; 83332.Rv0808; -.
DR MEROPS; C44.001; -.
DR PaxDb; P9WHQ7; -.
DR DNASU; 885085; -.
DR GeneID; 885085; -.
DR KEGG; mtu:Rv0808; -.
DR PATRIC; fig|83332.111.peg.895; -.
DR TubercuList; Rv0808; -.
DR eggNOG; COG0034; Bacteria.
DR OMA; ENAQPTF; -.
DR PhylomeDB; P9WHQ7; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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; -; 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 Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur;
KW Magnesium; Metal-binding; Purine biosynthesis; Reference proteome;
KW Transferase.
FT PROPEP 1..34
FT /evidence="ECO:0000250"
FT /id="PRO_0000029257"
FT CHAIN 35..527
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000029258"
FT DOMAIN 35..261
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 276
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 422
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 478
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 481
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
SQ SEQUENCE 527 AA; 56162 MW; A2FE9D1DD08FA572 CRC64;
MAVDSDYVTD RAAGSRQTVT GQQPEQDLNS PREECGVFGV WAPGEDVAKL TYYGLYALQH
RGQEAAGIAV ADGSQVLVFK DLGLVSQVFD EQTLAAMQGH VAIGHCRYST TGDTTWENAQ
PVFRNTAAGT GVALGHNGNL VNAAALAARA RDAGLIATRC PAPATTDSDI LGALLAHGAA
DSTLEQAALD LLPTVRGAFC LTFMDENTLY ACRDPYGVRP LSLGRLDRGW VVASETAALD
IVGASFVRDI EPGELLAIDA DGVRSTRFAN PTPKGCVFEY VYLARPDSTI AGRSVHAARV
EIGRRLAREC PVEADLVIGV PESGTPAAVG YAQESGVPYG QGLMKNAYVG RTFIQPSQTI
RQLGIRLKLN PLKEVIRGKR LIVVDDSIVR GNTQRALVRM LREAGAVELH VRIASPPVKW
PCFYGIDFPS PAELIANAVE NEDEMLEAVR HAIGADTLGY ISLRGMVAAS EQPTSRLCTA
CFDGKYPIEL PRETALGKNV IEHMLANAAR GAALGELAAD DEVPVGR
