MPTB_METJA
ID MPTB_METJA Reviewed; 249 AA.
AC Q58247;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase;
DE Short=H2N-cP phosphodiesterase;
DE Short=H2Neo-cP phosphodiesterase;
DE EC=3.1.4.56;
DE AltName: Full=7,8-dihydro-D-neopterin 2',3'-cyclic phosphate phosphodiesterase;
GN Name=mptB; OrderedLocusNames=MJ0837;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, GENE NAME,
RP PATHWAY, PH DEPENDENCE, SUBUNIT, AND MUTAGENESIS OF HIS-61; HIS-96 AND
RP ASP-167.
RX PubMed=19746965; DOI=10.1021/bi9010336;
RA Mashhadi Z., Xu H., White R.H.;
RT "An Fe2+-dependent cyclic phosphodiesterase catalyzes the hydrolysis of
RT 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate in methanopterin
RT biosynthesis.";
RL Biochemistry 48:9384-9392(2009).
CC -!- FUNCTION: Cyclic phosphodiesterase that hydrolyzes the cyclic phosphate
CC of 7,8-dihydroneopterin 2',3'-cyclic phosphate (H2N-cP) and converts it
CC to a mixture of 7,8-dihydroneopterin 2'-phosphate (H2N-2'P) and 7,8-
CC dihydroneopterin 3'-phosphate (H2N-3'P). Is also able to utilize other
CC phosphodiesters as substrates in vitro: hydrolysis of bis-pNPP and
CC pNPPC produces nitrophenyl phosphate, and that of 2',3'-cAMP produces
CC 3'-AMP. ATP, 3',5'-cAMP, GTP, 3',5'-cGMP, and 4',5'-cFMN cannot serve
CC as substrates. {ECO:0000269|PubMed:19746965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-
CC dihydroneopterin 3'-phosphate + H(+); Xref=Rhea:RHEA:35799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58762,
CC ChEBI:CHEBI:58854; EC=3.1.4.56;
CC Evidence={ECO:0000269|PubMed:19746965};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-
CC dihydroneopterin 2'-phosphate + H(+); Xref=Rhea:RHEA:35803,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58854,
CC ChEBI:CHEBI:72777; EC=3.1.4.56;
CC Evidence={ECO:0000269|PubMed:19746965};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19746965};
CC Note=Binds 1 Fe(2+) ion per subunit. Since MptB requires Fe2(+) for
CC activity, the Fe(2+) ion likely has a catalytic role. The enzyme is
CC also active under high concentrations of Mn(2+) in vitro.
CC {ECO:0000269|PubMed:19746965};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19746965};
CC Note=Binds 1 Zn(2+) ion per subunit. The Zn(2+) ion is proposed to have
CC a structural role. {ECO:0000269|PubMed:19746965};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5 with bis-pNPP as substrate.
CC {ECO:0000269|PubMed:19746965};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000269|PubMed:19746965}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:19746965}.
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DR EMBL; L77117; AAB98842.1; -; Genomic_DNA.
DR PIR; E64404; E64404.
DR RefSeq; WP_010870351.1; NC_000909.1.
DR AlphaFoldDB; Q58247; -.
DR STRING; 243232.MJ_0837; -.
DR EnsemblBacteria; AAB98842; AAB98842; MJ_0837.
DR GeneID; 1451723; -.
DR KEGG; mja:MJ_0837; -.
DR eggNOG; arCOG01861; Archaea.
DR HOGENOM; CLU_1109506_0_0_2; -.
DR OMA; IRICQAR; -.
DR OrthoDB; 56504at2157; -.
DR PhylomeDB; Q58247; -.
DR BioCyc; MetaCyc:MON-16557; -.
DR BRENDA; 3.1.4.56; 3260.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0044682; F:archaeal-specific GTP cyclohydrolase activity; IDA:MENGO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR TIGRFAMs; TIGR00277; HDIG; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Iron; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..249
FT /note="Dihydroneopterin 2',3'-cyclic phosphate
FT phosphodiesterase"
FT /id="PRO_0000107074"
FT DOMAIN 58..172
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT MUTAGEN 61
FT /note="H->N: Large reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:19746965"
FT MUTAGEN 96
FT /note="H->N: Slight reduction in catalytic activity with
FT H2N-cP and 2',3'-cAMP as substrates, but 2-fold increase in
FT activity with bis-pNPP."
FT /evidence="ECO:0000269|PubMed:19746965"
FT MUTAGEN 167
FT /note="D->N: Large reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:19746965"
SQ SEQUENCE 249 AA; 28523 MW; E8A59C478718E613 CRC64;
MERLIKLAEQ IKDEELRKKV IEFLKNPKAT HPGIVDTGIS VEEAPASINW HHRYEGGLIE
HTISVTKIAL KMADVLEEVY GVEVNRDYII AGALLHDIMK PYNYIRKEDG TFDHYDMFNL
DHLTLAVAEL YKRDFPIEVI KIVASHHGDH SPTRPNSIEA YIVHYADEAD SKINDVAVRV
CQARSRDLGI SEQEIYKAVN PLKVYEVRSR EGKLKTIEFL KDILKSIGII SEDEKKDENN
ESLENKESN
