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Database: UniProt
Entry: Q981B9
LinkDB: Q981B9
Original site: Q981B9 
ID   PURT_SACS2              Reviewed;         397 AA.
AC   Q981B9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   16-JAN-2019, entry version 95.
DE   RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Formate-dependent GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE            EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=GAR transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE            Short=GART 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
GN   Name=purT {ECO:0000255|HAMAP-Rule:MF_01643};
GN   OrderedLocusNames=SSO0026;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
OS   P2) (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
RA   Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
RA   De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
RA   Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
RA   Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
RA   Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes
CC       the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR),
CC       producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is
CC       provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
CC       {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-D-ribosyl)glycinamide =
CC         ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide +
CC         phosphate; Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58426, ChEBI:CHEBI:58457, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01643};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
CC       phospho-D-ribosyl)glycinamide (formate route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40393.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE006641; AAK40393.1; ALT_INIT; Genomic_DNA.
DR   PIR; B90142; B90142.
DR   RefSeq; WP_009989613.1; NC_002754.1.
DR   ProteinModelPortal; Q981B9; -.
DR   SMR; Q981B9; -.
DR   STRING; 273057.SSO0026; -.
DR   EnsemblBacteria; AAK40393; AAK40393; SSO0026.
DR   GeneID; 27426322; -.
DR   KEGG; sso:SSO0026; -.
DR   PATRIC; fig|273057.12.peg.29; -.
DR   eggNOG; arCOG01598; Archaea.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   InParanoid; Q981B9; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 57699at2157; -.
DR   BioCyc; SSOL273057:G1FZF-29-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01643; PurT; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005862; PurT.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    397       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_0000319288.
FT   DOMAIN      118    312       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     194    197       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION       21     22       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION      368    369       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   METAL       271    271       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       283    283       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   BINDING      81     81       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     113    113       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     154    154       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     202    202       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     290    290       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     361    361       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   397 AA;  44043 MW;  F1936F697D6D6783 CRC64;
     MEIGTPLFEG SKKILLLGSG ELGKEMAIEA QRMGLEVVAL DRYDLAPAMH VAHRKYVVDM
     MNPNAIKAVV KRERPDAIIA EIEAINTDAL IELESNGFRV VPNANAVKAC MNRIELRRFA
     AEKLKLPTTK YAFAENEEEV KRACKDIGFP CLIKPEMSSS GHGHVLVNKI ENVEEAYRES
     ISHARGKSRR VIVEEFVKID TELTVLTYRY HSNSDSIITK TIEPIEHKRP SYYYVESWHP
     SNVSQGVKET ARGIAQKVAE ELGGLGIYGV EIIVSGNRIL FSEVAPRPHD TGLVTLASSD
     INEFQIHVRS AIGLPTPEVK LVSPAASHVI LAQTENVWGP KFLNIEKAME IPGVQVRLFG
     KPVTYEKRRM GVVLATGNSV EEALEKVRKA SSIILVK
//
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