ID A0A2T0VGJ5_9MICO Unreviewed; 420 AA.
AC A0A2T0VGJ5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=B0I08_103392 {ECO:0000313|EMBL:PRY69184.1};
OS Glaciihabitans tibetensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Glaciihabitans.
OX NCBI_TaxID=1266600 {ECO:0000313|EMBL:PRY69184.1, ECO:0000313|Proteomes:UP000237983};
RN [1] {ECO:0000313|EMBL:PRY69184.1, ECO:0000313|Proteomes:UP000237983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12484 {ECO:0000313|EMBL:PRY69184.1,
RC ECO:0000313|Proteomes:UP000237983};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC molybdopterin with the concomitant release of AMP.
CC {ECO:0000256|ARBA:ARBA00002901, ECO:0000256|RuleBase:RU365090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001529};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU365090};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC ECO:0000256|RuleBase:RU365090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRY69184.1}.
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DR EMBL; PVTL01000003; PRY69184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0VGJ5; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000237983; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00887; MoeA; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU365090};
KW Metal-binding {ECO:0000256|RuleBase:RU365090};
KW Molybdenum {ECO:0000256|RuleBase:RU365090};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|RuleBase:RU365090};
KW Reference proteome {ECO:0000313|Proteomes:UP000237983};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:PRY69184.1}.
FT DOMAIN 193..331
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 420 AA; 43268 MW; F556E824FCEC027D CRC64;
MTRDDDCAPS ARVYSRTVAE HLAIVLDAVP VLGAERRSLD AARGLVAAED VRSATATPPF
DNSAMDGYAV HSADLRGVSE SAPVALVVVA DLPAGSADNP TIDFGQAARI MTGAPIPDGI
DAVVPIEHTD EGTATVLVFR PPRAGAHLRR AGEDAAAGDR VVSAGSVMWP TRLAAAASAG
ADAILVHPAP RVAVISTGSE LVAPGHPLRR GQIPDSNSFL LSAAVTEAGG VATRIGAVPD
DPDALREVLA RIAPTVDAMV LSGGVSVGAF DVVKAVLAPL DTMFFGPILM QPGKPQGFGR
LPQGPVVFAL PGNPVSAYVS FEAFVRPALL RMAGHTSLHR RTITAVADDA WTCPAGRMQY
MPVVVEGEPG RERVKRATSG GSSSHLIAGL GRSTGLAVIP EQLDRVEAGD RLTVMVTTSP
//
