NASC_HALMT
ID NASC_HALMT Reviewed; 210 AA.
AC I3R636; Q703N3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable molybdenum cofactor guanylyltransferase;
DE Short=MoCo guanylyltransferase;
DE EC=2.7.7.77;
DE AltName: Full=GTP:molybdopterin guanylyltransferase;
DE AltName: Full=Mo-MPT guanylyltransferase;
DE AltName: Full=Molybdopterin guanylyltransferase;
DE AltName: Full=Molybdopterin-guanine dinucleotide synthase;
DE Short=MGD synthase;
GN Name=nasC; Synonyms=mobA; OrderedLocusNames=HFX_2004; ORFNames=C439_11798;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=16182473; DOI=10.1016/j.gene.2005.07.011;
RA Lledo B., Marhuenda-Egea F.C., Martinez-Espinosa R.M., Bonete M.J.;
RT "Identification and transcriptional analysis of nitrate assimilation genes
RT in the halophilic archaeon Haloferax mediterranei.";
RL Gene 361:80-88(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT)
CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine
CC dinucleotide (Mo-MGD) cofactor. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin
CC guanine dinucleotide; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302,
CC ChEBI:CHEBI:71310; EC=2.7.7.77;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition and
CC specific binding, while the C-terminal domain determines the specific
CC binding to the target protein. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000305}.
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DR EMBL; AJ621500; CAF19044.1; -; Genomic_DNA.
DR EMBL; CP001868; AFK19696.1; -; Genomic_DNA.
DR EMBL; AOLO01000009; EMA00018.1; -; Genomic_DNA.
DR RefSeq; WP_004059342.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R636; -.
DR SMR; I3R636; -.
DR STRING; 523841.HFX_2004; -.
DR EnsemblBacteria; AFK19696; AFK19696; HFX_2004.
DR EnsemblBacteria; EMA00018; EMA00018; C439_11798.
DR GeneID; 40155086; -.
DR KEGG; hme:HFX_2004; -.
DR eggNOG; arCOG01872; Archaea.
DR HOGENOM; CLU_055597_2_1_2; -.
DR OrthoDB; 78708at2157; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02503; MobA; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_00316; MobA; 1.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR013482; Molybde_CF_guanTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Transferase.
FT CHAIN 1..210
FT /note="Probable molybdenum cofactor guanylyltransferase"
FT /id="PRO_0000428893"
FT BINDING 18..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 82..86
FT /note="DSHPD -> TLTQN (in Ref. 1; CAF19044)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..189
FT /note="NVLDGREVQAHA -> TSWTGAKCRHTP (in Ref. 1; CAF19044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 22257 MW; AF3F51033301FE0F CRC64;
MAEQSSRNLD TGRAGIILAG GRSRRFDGID KATAPVGGRP MIHRVAASLD PAVDELVINC
RADQRDTFAA ALSDFDVRFA EDSHPDHGPV FGLRTAVRAS NAEYAAILPC DMPLVPTGFI
SHLFGRVQGG TGVIPSVSET PVPLPSVVHC RAGEVACTET IRAGSDRLKD VMSTLGVNVL
DGREVQAHAG LDAFSNVNTI DDLRALSSRR
