(data stored in ACNUC7421 zone)

SWISSPROT: A0LEW7_SYNFM

ID   A0LEW7_SYNFM            Unreviewed;       468 AA.
AC   A0LEW7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|PIRNR:PIRNR000485};
DE            Short=ATase {ECO:0000256|PIRNR:PIRNR000485};
DE            EC=2.4.2.14 {ECO:0000256|PIRNR:PIRNR000485};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|PIRNR:PIRNR000485};
GN   OrderedLocusNames=Sfum_0268 {ECO:0000313|EMBL:ABK15969.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15969.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15969.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
CC         = 5-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;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000485};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000485-3};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {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|PIRNR:PIRNR000485}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       purine/pyrimidine phosphoribosyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR000485}.
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DR   EMBL; CP000478; ABK15969.1; -; Genomic_DNA.
DR   RefSeq; WP_011697142.1; NC_008554.1.
DR   STRING; 335543.Sfum_0268; -.
DR   EnsemblBacteria; ABK15969; ABK15969; Sfum_0268.
DR   KEGG; sfu:Sfum_0268; -.
DR   eggNOG; ENOG4107UBB; Bacteria.
DR   eggNOG; COG0034; LUCA.
DR   HOGENOM; HOG000010521; -.
DR   KO; K00764; -.
DR   OMA; IKYTPTW; -.
DR   OrthoDB; 267682at2; -.
DR   BioCyc; SFUM335543:G1G7I-271-MONOMER; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.60.20.10; -; 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   Pfam; PF13537; GATase_7; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEW7.
DR   SWISS-2DPAGE; A0LEW7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000485,
KW   ECO:0000313|EMBL:ABK15969.1}; Iron {ECO:0000256|PIRSR:PIRSR000485-3};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR000485-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000485-3};
KW   Purine biosynthesis {ECO:0000256|PIRNR:PIRNR000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000485,
KW   ECO:0000313|EMBL:ABK15969.1}.
FT   DOMAIN        2    217       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   METAL       232    232       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       379    379       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       457    457       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       460    460       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
SQ   SEQUENCE   468 AA;  52308 MW;  5F13BD03D29FB145 CRC64;
     MGGLFGIVSR DDCVSDLFYG TDYHSHLGTR LGGMAVCNSK GIQRSIHNIE NSYFRTRFES
     DLARFSGNKG VGVISDTDPQ PLIARSHLGT FGIVTVGKIN NMEELLHKAF DERRSFFDTA
     GGVVGPSEMV AKLICSEDNL EDGIRKVQAS IRGSCSLLLL TDDGIYAARD RLGRTPLVIG
     RRNGARAVSS ESCAFPNLGF EVERFLGPGE VVYVACDGWE QRLPPGRDMQ ICSFLWVYYG
     YPASDYEGIN VEFVRNACGC ALARDDDAEV DYVAGIPDSG IGHALGYANE RRIPYRRPFV
     KYTPTWPRSF MPQDQRLRDL VARMKLIPVR SLIEGKRLLF CEDSIVRGTQ LKDNIQILFD
     YGAREVHMRP ACPTLVFPCE FLNFSASRST EDLIGRKIIH ELENGRDKDL QSYITAGSKK
     NLAMVEEIRK RLRLTTLRYQ RLDDLVASIG LPKEKLCTHC WDGSSKGA
//

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