(data stored in SCRATCH zone)

SWISSPROT: C7QJA7_CATAD

ID   C7QJA7_CATAD            Unreviewed;       505 AA.
AC   C7QJA7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   30-AUG-2017, entry version 64.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE            Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931};
DE            EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE            Short=GPATase {ECO:0000256|HAMAP-Rule:MF_01931};
GN   Name=purF {ECO:0000256|HAMAP-Rule:MF_01931};
GN   OrderedLocusNames=Caci_0296 {ECO:0000313|EMBL:ACU69249.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69249.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69249.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine.
CC       {ECO:0000256|HAMAP-Rule:MF_01931}.
CC   -!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate +
CC       L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate
CC       + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01931,
CC       ECO:0000256|PIRNR:PIRNR000485}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01931};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01931};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01931,
CC         ECO:0000256|PIRSR:PIRSR000485-3};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-3};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_01931,
CC       ECO:0000256|PIRNR:PIRNR000485}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       purine/pyrimidine phosphoribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
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DR   EMBL; CP001700; ACU69249.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QJA7; -.
DR   STRING; 479433.Caci_0296; -.
DR   MEROPS; C44.A03; -.
DR   EnsemblBacteria; ACU69249; ACU69249; Caci_0296.
DR   KEGG; cai:Caci_0296; -.
DR   eggNOG; ENOG4105CBA; Bacteria.
DR   eggNOG; COG0034; LUCA.
DR   HOGENOM; HOG000033688; -.
DR   KO; K00764; -.
DR   OMA; HVYFARP; -.
DR   OrthoDB; POG091H0061; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
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; 3.60.20.10; -; 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; PF13537; GATase_7; 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.
PE   3: Inferred from homology;
DR   PRODOM; C7QJA7.
DR   SWISS-2DPAGE; C7QJA7.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01931};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:ACU69249.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-
KW   3};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRSR:PIRSR000485-3};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01931};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRSR:PIRSR000485-3};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:ACU69249.1}.
FT   DOMAIN       29    254       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   ACT_SITE     29     29       For GATase activity. {ECO:0000256|PIRSR:
FT                                PIRSR000485-1}.
FT   ACT_SITE     29     29       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931}.
FT   METAL       269    269       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       316    316       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931}.
FT   METAL       378    378       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931}.
FT   METAL       379    379       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931}.
FT   METAL       415    415       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       466    466       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       469    469       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
SQ   SEQUENCE   505 AA;  54346 MW;  84CFB32809AA017B CRC64;
     MIHPSGFRPG DGRLTHELDP QDTGPQDACG VFGVWAPGEE VAKLAYFGLY ALQHRGQESA
     GIAVSNGKQI LVYKDMGLVS QVFDEATLQS LQGYLAIGHA RYSTTGSSVW ENAQPTFRAT
     AHGAVALGHN GNLTNTGELA RLAAERRTTS GAGDKHAMTS DTGLMTELLA SYSDRSLEDA
     AAEVLPQLRG AFSLVFMDET TLYAARDPQG VRPLMLGRLD RGWVVASEQA ALDTVGASFI
     REIEPGELIA VDENGLRSRH FAEPQPKGCV FEYVYLARPD ATISGRNVHA ARVEMGRTLA
     REAPVEADLV IATPESGTPA AIGFAEESGI PFGQGFVKNA YVGRTFIQPS QTLRQLGVRL
     KLNALREVIE GKRLVVVDDS IVRGNTQRAV SKMLREAGAT EVHLRISSPP VKWPCFYGID
     FATRAELIAN GLNTDEIAKS IGADSLAYIT LDGMTAATHQ PADRLCRACF DGVYPIALPE
     DELLGKHLLE ISVDPLAHTD ALSRP
//

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