MPNS_NITMS
ID MPNS_NITMS Reviewed; 457 AA.
AC A9A1T2;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Methylphosphonate synthase;
DE EC=1.13.11.73;
GN Name=mpnS; OrderedLocusNames=Nmar_0155;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND COFACTOR.
RC STRAIN=SCM1;
RX PubMed=22936780; DOI=10.1126/science.1219875;
RA Metcalf W.W., Griffin B.M., Cicchillo R.M., Gao J., Janga S.C., Cooke H.A.,
RA Circello B.T., Evans B.S., Martens-Habbena W., Stahl D.A.,
RA van der Donk W.A.;
RT "Synthesis of methylphosphonic acid by marine microbes: a source for
RT methane in the aerobic ocean.";
RL Science 337:1104-1107(2012).
CC -!- FUNCTION: Catalyzes the conversion of 2-hydroxyethylphosphonate into
CC methylphosphonate in the methylphosphonate biosynthesis pathway.
CC {ECO:0000269|PubMed:22936780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyethylphosphonate + O2 = H(+) + hydrogencarbonate +
CC methylphosphonate; Xref=Rhea:RHEA:34615, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17544, ChEBI:CHEBI:60991,
CC ChEBI:CHEBI:68684; EC=1.13.11.73;
CC Evidence={ECO:0000269|PubMed:22936780};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:22936780};
CC -!- PATHWAY: Phosphorus metabolism; phosphonate biosynthesis.
CC {ECO:0000269|PubMed:22936780}.
CC -!- MISCELLANEOUS: The existence of the methylphosphonate biosynthesis
CC pathway in marine microbes may explain the supersaturation of the
CC aerobic ocean with methane. Methane is probably released following
CC degradation of methylphosphonate produced by MpnS (PubMed:22936780).
CC {ECO:0000305|PubMed:22936780}.
CC -!- SIMILARITY: Belongs to the non-heme iron-dependent dioxygenase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=An unusual chemistry - Issue
CC 160 of May 2014;
CC URL="https://web.expasy.org/spotlight/back_issues/160/";
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DR EMBL; CP000866; ABX12053.1; -; Genomic_DNA.
DR PDB; 6B9S; X-ray; 2.37 A; A/B/C/D/E/F/G/H=1-457.
DR PDB; 6B9T; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-457.
DR PDBsum; 6B9S; -.
DR PDBsum; 6B9T; -.
DR AlphaFoldDB; A9A1T2; -.
DR SMR; A9A1T2; -.
DR STRING; 436308.Nmar_0155; -.
DR EnsemblBacteria; ABX12053; ABX12053; Nmar_0155.
DR KEGG; nmr:Nmar_0155; -.
DR eggNOG; arCOG01865; Archaea.
DR HOGENOM; CLU_598026_0_0_2; -.
DR BioCyc; MetaCyc:MON-17793; -.
DR UniPathway; UPA00960; -.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR GO; GO:0032923; P:organic phosphonate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 2.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; DNA-binding; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..457
FT /note="Methylphosphonate synthase"
FT /id="PRO_0000422033"
FT DOMAIN 23..74
FT /note="HTH cro/C1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DOMAIN 247..301
FT /note="HTH cro/C1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 32..50
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 258..277
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 149..165
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:6B9T"
FT STRAND 406..419
FT /evidence="ECO:0007829|PDB:6B9T"
FT TURN 421..425
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6B9T"
FT HELIX 439..443
FT /evidence="ECO:0007829|PDB:6B9T"
SQ SEQUENCE 457 AA; 52054 MW; B302C62CA53AAA84 CRC64;
MEKKIDFKPD SYLIRSGNNF LGILNDIKRR PEDAANELGV SIEEINSIIS GKQKISPSLI
EKAVNIWPVN ERDFYIVSDD CSSGILIMTS QDSIKSSRIM ERAGKPYYEY RDTAMSKTAP
FRPEWILELC KVENNDPENP KAQWNNGHFM HQFTYFIGEV NFYYKDPEGK KHVAIMNTGD
SMYITPFTPH TFTTRDGASQ NGLILALTYG SKLTGDIQQE LSSLSLDCGS QYALDFTNHE
NASLSLLEYY FELSNLTKEK FAKRTNFSME TLADFFTKKK LPTFDELKII AKALNVNSRD
LMPNDLTESK VIVKTHDQCD HWKYPESGNY EFYELASTTA LPHSKAFEID VSSSEDLNLD
LKVGLHQYVY NIGDSALTIN WNYENKTYQK SLNPGDSAYI KPFVPHNFRG NGKILILRIG
GKISGDSQRE LSFVGRENTQ RAISETMQWF DPKGSNS
