ID A0A0A1D3T4_9MICC Unreviewed; 457 AA.
AC A0A0A1D3T4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=ART_4279 {ECO:0000313|EMBL:AIY03878.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY03878.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIY03878.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY03878.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
RL Submitted (APR-2014) 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}.
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DR EMBL; CP007595; AIY03878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1D3T4; -.
DR STRING; 1494608.ART_4279; -.
DR KEGG; arm:ART_4279; -.
DR HOGENOM; CLU_010186_7_0_11; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000030301; Chromosome.
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 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:UP000030301};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 216..372
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 457 AA; 46906 MW; E113ADC9C86F2C0D CRC64;
MPGGACGKGT MHRSVAEHQE AVTELLRRSW AGFPSPVMDD GGTPVPLSLA RGRVLAQDLV
AGMDLPPFTN SQMDGYAMWV DPALAGSERA RPAQSESVDS GKSTSYVVGE TIAAGAVPRE
LPPGTAAPIM TGAMLPARAN AVVPVERAVP ALFAEAGATV ELPATAPDAF VRAQGSDVQR
GSTVIAAGTI LNAAHLGLAA ALGCTELVVR RRVRVLLLTT GDEVLAPGDP AAANGLPPGM
IFDANGALLR AALEESGVEV LHSHMVRDEP SALLRLLESR VGHAPAHSGA PEPTCDLVVS
VGGISAGAFE VVRQALGSAG KHAEMEFLHV ALQPGGPQGL GTFRGVPFLA FPGNPVSSYV
SLELFLRPAL SALLGAPTPR HRVVAALEHP LTSPLGKHQI RRGVYSGPEF ESAPSVHEVG
GTSSHLLGSL GRANALIQVP AGVTALQAGA KVEVWLL
//
