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Database: UniProt
Entry: A6Q186
LinkDB: A6Q186
Original site: A6Q186 
ID   PURT_NITSB              Reviewed;         388 AA.
AC   A6Q186;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   16-JAN-2019, entry version 77.
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=NIS_0130;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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}.
DR   EMBL; AP009178; BAF69245.1; -; Genomic_DNA.
DR   RefSeq; WP_011979671.1; NC_009662.1.
DR   ProteinModelPortal; A6Q186; -.
DR   SMR; A6Q186; -.
DR   STRING; 387092.NIS_0130; -.
DR   PRIDE; A6Q186; -.
DR   EnsemblBacteria; BAF69245; BAF69245; NIS_0130.
DR   KEGG; nis:NIS_0130; -.
DR   eggNOG; ENOG4108HH9; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 1677960at2; -.
DR   BioCyc; NSP387092:G1G2O-141-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001118; Chromosome.
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   TIGRFAMs; TIGR01142; purT; 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    388       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_0000319190.
FT   DOMAIN      118    306       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     159    164       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   NP_BIND     193    196       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION       21     22       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION      359    360       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   METAL       265    265       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       277    277       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     201    201       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     284    284       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     352    352       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   388 AA;  43101 MW;  79B017B4E49BC53F CRC64;
     MQFPAPLKSN SIKFLLLGSG ELGKEVAIEA QRLGIEVVAV DRYPNAPAHL VAHRSYVIDM
     KSKEQVLEVI FREKPDYILP EIEAINIEAL FEAEERGFRV IPNAEAVNKT MNRKNIRKFA
     AEELGLKTSQ YRFVSSFEGL QEAARTLGFP CVIKPVMSSS GHGQSIARNE ADLERSWEIA
     KEARGDASEL IVEEFIDFDY EITLLTARNE TGTVFCPPIG HIQKDGDYIF SWQPMQMSET
     ALQKAKEIAK TITDGLGGRG IFGVELFVKG DEVYFSEVSP RPHDTGMVTM ITQSQSEFAL
     HVRAVLGLGL GFTFYTPGAS AAYKAKHESF TPVIEADESV FDQESFLRVF GKPESHEGRR
     MAVVLTLAET AEQALQKANE LIAKVSDQ
//
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