MOAB_PYRFU
ID MOAB_PYRFU Reviewed; 169 AA.
AC Q8U3T3;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Molybdopterin adenylyltransferase;
DE Short=MPT adenylyltransferase;
DE EC=2.7.7.75;
GN Name=moaB; OrderedLocusNames=PF0372;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-32; ASP-56; ASP-57 AND
RP SER-112, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18154309; DOI=10.1021/bi7020487;
RA Bevers L.E., Hagedoorn P.L., Santamaria-Araujo J.A., Magalon A.,
RA Hagen W.R., Schwarz G.;
RT "Function of MoaB proteins in the biosynthesis of the molybdenum and
RT tungsten cofactors.";
RL Biochemistry 47:949-956(2008).
CC -!- FUNCTION: Catalyzes the adenylation of molybdopterin as part of the
CC biosynthesis of the molybdenum-cofactor. {ECO:0000269|PubMed:18154309}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC ChEBI:CHEBI:62727; EC=2.7.7.75;
CC Evidence={ECO:0000269|PubMed:18154309};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=225 uM for ATP {ECO:0000269|PubMed:18154309};
CC Vmax=18.6 pmol/min/mg enzyme {ECO:0000269|PubMed:18154309};
CC Temperature dependence:
CC Optimum temperature is >80 degrees Celsius.
CC {ECO:0000269|PubMed:18154309};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:18154309}.
CC -!- SIMILARITY: Belongs to the MoaB/Mog family. {ECO:0000305}.
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DR EMBL; AE009950; AAL80496.1; -; Genomic_DNA.
DR RefSeq; WP_011011486.1; NZ_CP023154.1.
DR PDB; 4LHB; X-ray; 2.50 A; A/B/C=1-169.
DR PDBsum; 4LHB; -.
DR AlphaFoldDB; Q8U3T3; -.
DR SMR; Q8U3T3; -.
DR STRING; 186497.PF0372; -.
DR PRIDE; Q8U3T3; -.
DR EnsemblBacteria; AAL80496; AAL80496; PF0372.
DR GeneID; 41712162; -.
DR KEGG; pfu:PF0372; -.
DR PATRIC; fig|186497.12.peg.387; -.
DR eggNOG; arCOG00214; Archaea.
DR HOGENOM; CLU_077358_2_3_2; -.
DR OMA; TGWDGIL; -.
DR OrthoDB; 108340at2157; -.
DR PhylomeDB; Q8U3T3; -.
DR BioCyc; MetaCyc:MON-21135; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; -; 1.
DR InterPro; IPR012245; MoaB.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR PANTHER; PTHR43232; PTHR43232; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF006443; MoaB; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; SSF53218; 1.
DR TIGRFAMs; TIGR00177; molyb_syn; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Molybdenum cofactor biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..169
FT /note="Molybdopterin adenylyltransferase"
FT /id="PRO_0000392068"
FT MUTAGEN 32
FT /note="D->A: 10-fold reduction of activity."
FT /evidence="ECO:0000269|PubMed:18154309"
FT MUTAGEN 56
FT /note="D->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:18154309"
FT MUTAGEN 57
FT /note="D->E: No effect on activity."
FT /evidence="ECO:0000269|PubMed:18154309"
FT MUTAGEN 112
FT /note="S->A: Little effect on activity."
FT /evidence="ECO:0000269|PubMed:18154309"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4LHB"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:4LHB"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4LHB"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4LHB"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:4LHB"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:4LHB"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:4LHB"
FT HELIX 146..167
FT /evidence="ECO:0007829|PDB:4LHB"
SQ SEQUENCE 169 AA; 18573 MW; 65298519B489642A CRC64;
MGVEEHKKEA PKTFKFGVIT VSDKGAKGER EDKSGPLIIE ELSKLGEHVY YKIVPDDKIE
VLIALFEAIK SGADVVVTTG GTGITRRDIT IESIKPLFDK ELSFGEVFRA KSYEEVGYAT
VLTRATAGII RGQERIVVVF SLPGSVNAVK TGLEIIKSEV FHILKHARE
