(data stored in SCRATCH zone)

SWISSPROT: PURT_PROMP

ID   PURT_PROMP              Reviewed;         390 AA.
AC   Q7V179;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   11-DEC-2019, entry version 114.
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}; OrderedLocusNames=PMM1004;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae; Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the
CC       transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing
CC       5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by
CC       PurU via hydrolysis of 10-formyl-tetrahydrofolate. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-D-ribosyl)glycinamide = ADP +
CC         H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58426,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01643};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC       ribosyl)glycinamide (formate route): step 1/1. {ECO:0000255|HAMAP-
CC       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; BX548174; CAE19463.1; -; Genomic_DNA.
DR   RefSeq; WP_011132636.1; NC_005072.1.
DR   SMR; Q7V179; -.
DR   STRING; 59919.PMM1004; -.
DR   PRIDE; Q7V179; -.
DR   EnsemblBacteria; CAE19463; CAE19463; PMM1004.
DR   KEGG; pmm:PMM1004; -.
DR   eggNOG; ENOG4108HH9; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 1677960at2; -.
DR   BioCyc; PMAR59919:TX50_RS05370-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001026; 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   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01142; purT; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7V179.
DR   SWISS-2DPAGE; Q7V179.
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Purine biosynthesis; Transferase.
FT   CHAIN           1..390
FT                   /note="Formate-dependent phosphoribosylglycinamide
FT                   formyltransferase"
FT                   /id="PRO_0000319207"
FT   DOMAIN          115..305
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   NP_BIND         156..161
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   NP_BIND         191..194
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   REGION          18..19
FT                   /note="5'-phosphoribosylglycinamide binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   REGION          360..361
FT                   /note="5'-phosphoribosylglycinamide binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   METAL           264
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   METAL           276
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         78
FT                   /note="5'-phosphoribosylglycinamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         110
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         151
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         199
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         283
FT                   /note="5'-phosphoribosylglycinamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         353
FT                   /note="5'-phosphoribosylglycinamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
SQ   SEQUENCE   390 AA;  43724 MW;  57FC76FA2C6883AC CRC64;
     MSSFKFIPKK ILLLGSGELG KELVVEAKRL GLEVIAIDKY ENAPAMQLAD NSFVIDMSDK
     EILKKKIKEL NPDFVVPEIE ALSIEALKEL EDEGINIVPN ARTVEITMNR DKIRDLASKE
     LNIKTAKFSY VFNVDELEIK SSEIGFPLLI KPLMSSSGKG QSLVNRKEDL LLAWNDALKN
     SRGKIVGVIL EEFLNFDYEF TLLTIRKTSG ENIFCEPIGH EQYKGDYQCS WQPLDMNQSL
     INEARKMTTK ILNNLNGSGI YGVEFFVRGK EVIFSELSPR PHDTGMVTLV SQNINEFELH
     LRAFLNLPIP NISLLKPSAT RVIISDKESN TPSYSGLNEA LELENTKVLI FGKPTAKKGR
     RMGVVLSTDD DLNIARENAD KSALKIKIVS
//

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