ID   PHPF_STRVT              Reviewed;         184 AA.
AC   Q5IW36; D9XF40;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Phosphonoformate cytidylyltransferase {ECO:0000305};
DE            EC=2.7.7.93 {ECO:0000269|PubMed:17632514};
GN   Name=phpF {ECO:0000303|PubMed:15616300};
GN   ORFNames=SSQG_01037 {ECO:0000312|EMBL:EFL30519.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=591159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=15574905; DOI=10.1128/aem.70.12.7093-7102.2004;
RA   Schwartz D., Berger S., Heinzelmann E., Muschko K., Welzel K.,
RA   Wohlleben W.;
RT   "Biosynthetic gene cluster of the herbicide phosphinothricin tripeptide
RT   from Streptomyces viridochromogenes Tu494.";
RL   Appl. Environ. Microbiol. 70:7093-7102(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=15616300; DOI=10.1128/aac.49.1.230-240.2005;
RA   Blodgett J.A., Zhang J.K., Metcalf W.W.;
RT   "Molecular cloning, sequence analysis, and heterologous expression of the
RT   phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces
RT   viridochromogenes DSM 40736.";
RL   Antimicrob. Agents Chemother. 49:230-240(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=17632514; DOI=10.1038/nchembio.2007.9;
RA   Blodgett J.A., Thomas P.M., Li G., Velasquez J.E., van der Donk W.A.,
RA   Kelleher N.L., Metcalf W.W.;
RT   "Unusual transformations in the biosynthesis of the antibiotic
RT   phosphinothricin tripeptide.";
RL   Nat. Chem. Biol. 3:480-485(2007).
CC   -!- FUNCTION: Catalyzes the displacement of the beta- and gamma-phosphates
CC       of CTP by phosphonoformate to produce CMP-5'-phosphonoformate, an
CC       intermediate in the biosynthesis of phosphinothricin tripeptide (PTT).
CC       PTT is both a natural-product antibiotic and potent herbicide.
CC       {ECO:0000269|PubMed:17632514}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + phosphonoformate = CMP-5'-phosphonoformate +
CC         diphosphate; Xref=Rhea:RHEA:49428, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:91254, ChEBI:CHEBI:91255; EC=2.7.7.93;
CC         Evidence={ECO:0000269|PubMed:17632514};
CC   -!- PATHWAY: Antibiotic biosynthesis; phosphinothricin biosynthesis.
CC       {ECO:0000269|PubMed:17632514}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to produce PTT when
CC       grown in MYG broth supplemented with 0.5 mM phosphonoformate.
CC       {ECO:0000269|PubMed:17632514}.
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DR   EMBL; X65195; CAJ14046.1; -; Genomic_DNA.
DR   EMBL; AY632421; AAU00081.1; -; Genomic_DNA.
DR   EMBL; GG657757; EFL30519.1; -; Genomic_DNA.
DR   RefSeq; WP_003988634.1; NZ_GG657757.1.
DR   SMR; Q5IW36; -.
DR   STRING; 591159.ACEZ01000045_gene2946; -.
DR   EnsemblBacteria; EFL30519; EFL30519; SSQG_01037.
DR   KEGG; ag:AAU00081; -.
DR   eggNOG; COG1056; Bacteria.
DR   HOGENOM; CLU_108783_0_0_11; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; MetaCyc:MON-15036; -.
DR   BRENDA; 2.7.7.93; 6116.
DR   UniPathway; UPA00168; -.
DR   Proteomes; UP000004184; Unassembled WGS sequence.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..184
FT                   /note="Phosphonoformate cytidylyltransferase"
FT                   /id="PRO_0000453524"
SQ   SEQUENCE   184 AA;  20787 MW;  AED65C1C6A73382A CRC64;
     MSAEQIAGTG VIHGRFQPLH LGHLEYLLAG AERCRTLVVG ITNPDPWTTT EETTDPERGL
     PESNPCTFYE RYLMVEGALT EAGVSHERLR IVPFPHSFPE RLAHYAPADA RYFVTVYDDW
     GDAKLDRFHA LGLRTEVMWR RTDKPVSGGR VRRSIAEGQP WEHLVPPAVA RVVKECGIDE
     RIRA