PHPC_STRVT
ID PHPC_STRVT Reviewed; 395 AA.
AC D9XF45; Q5IW41;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Phosphonoacetaldehyde reductase;
DE EC=1.1.1.309 {ECO:0000269|PubMed:17632514};
GN Name=phpC; Synonyms=adhP; ORFNames=SSQG_01042;
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=8593056; DOI=10.1128/aem.62.2.570-577.1996;
RA Schwartz D., Alijah R., Nussbaumer B., Pelzer S., Wohlleben W.;
RT "The peptide synthetase gene phsA from Streptomyces viridochromogenes is
RT not juxtaposed with other genes involved in nonribosomal biosynthesis of
RT peptides.";
RL Appl. Environ. Microbiol. 62:570-577(1996).
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 reduction of phosphonoacetaldehyde to 2-
CC hydroxyethylphosphonate, a step in the biosynthesis of phosphinothricin
CC tripeptide. Phosphinothricin tripeptide is both a natural-product
CC antibiotic and potent herbicide. Can use both NAD and NADP but the
CC preferred substrate is NAD. {ECO:0000269|PubMed:17632514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyethylphosphonate + NAD(+) = H(+) + NADH +
CC phosphonoacetaldehyde; Xref=Rhea:RHEA:28078, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58383,
CC ChEBI:CHEBI:60991; EC=1.1.1.309;
CC Evidence={ECO:0000269|PubMed:17632514};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Antibiotic biosynthesis; phosphinothricin biosynthesis.
CC {ECO:0000269|PubMed:17632514}.
CC -!- DISRUPTION PHENOTYPE: Cells retain the ability to produce
CC phosphinothricin tripeptide when grown in liquid culture but, the
CC amount of PTT produced is lower. {ECO:0000269|PubMed:17632514}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X65195; CAJ14041.1; -; Genomic_DNA.
DR EMBL; AY632421; AAU00078.1; -; Genomic_DNA.
DR EMBL; GG657757; EFL30524.1; -; Genomic_DNA.
DR RefSeq; WP_003988639.1; NZ_GG657757.1.
DR AlphaFoldDB; D9XF45; -.
DR SMR; D9XF45; -.
DR STRING; 591159.ACEZ01000045_gene2951; -.
DR EnsemblBacteria; EFL30524; EFL30524; SSQG_01042.
DR KEGG; ag:AAU00078; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_11; -.
DR OrthoDB; 1456634at2; -.
DR BioCyc; MetaCyc:MON-15039; -.
DR UniPathway; UPA00168; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08182; HEPD; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR035873; PhpC.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Iron; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..395
FT /note="Phosphonoacetaldehyde reductase"
FT /id="PRO_0000418762"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 395 AA; 40987 MW; 8E3C32088C1A4F4C CRC64;
MTAVFPGELL LAEGIHEIAR VTALLSGPLR RAPRVAQVVG PGFAGRPWAP RLTDALRPLD
PTVVVHDGPT TPDSVAALAR QLRAIRADVA VAIGGGTVMD AAKAAAALAD GGPPDADRVR
QACAAGPAAG DTPPAVRVVA VPTTAGTGAE ATPFATLWDL KHRRKLSLTG PRVRPSAAVL
APELLAGLGR RALATGILDA LCQGAEASWS IRSTPESIRW GTSAVTLAAE ALDQVQDDAP
DAAARLALQR AAHHSGRAIA LAQTSSCHAI SYPLTLRLGL AHGHACGVTL GRLLRYNHAV
PAGDCADPRG TGHVRRVLDA LAAPLGGTPA RAALRVERFI TACGLTPYDA LDVDHRSLAA
EAVTYPRCHD NPRRLDRESL GRLLGERSEM EETCG
