ID A0A109FDE1_9BASI Unreviewed; 656 AA.
AC A0A109FDE1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=molybdopterin adenylyltransferase {ECO:0000256|ARBA:ARBA00012509};
DE EC=2.7.7.75 {ECO:0000256|ARBA:ARBA00012509};
GN ORFNames=RHOSPDRAFT_30086 {ECO:0000313|EMBL:KWU42444.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU42444.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU42444.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU42444.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC molybdate is inserted into adenylated molybdopterin and AMP is
CC released. {ECO:0000256|RuleBase:RU365090}.
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; Evidence={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;
CC Evidence={ECO:0000256|RuleBase:RU365090};
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|RuleBase:RU365090}.
CC -!- SIMILARITY: Belongs to the MoeA family.
CC {ECO:0000256|RuleBase:RU365090}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
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DR EMBL; KQ954508; KWU42444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FDE1; -.
DR STRING; 1305733.A0A109FDE1; -.
DR OrthoDB; 1908533at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; 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; 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; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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:UP000062823};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 408..555
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 656 AA; 69110 MW; 9362FC614D3BD58C CRC64;
MATSASAAPV LGPAVLLLLG GRSTRMGQPK HLLPHPRSGK PLYQHHIETL LEVAADGIFP
GGVFVSGRRE QMTDLFLPEG VQAILDDPET NGEIGPAAGI LQAAAAKPDT TWLILAVDLP
FITRGSILHL LSAHSTESPV SLYLHSNDGN PEPLFSIWTP TALAQLRSNC RAGKSGPCRA
AKDVWGGKIG PGKGGVEVPS EEWITDADTP DEWRAVQRRL TPSESQPEED GTSSLLAGVG
RATEQDLYAV LPHPLADNSA MDGFAVNARL LVGASRDSPV FLPILGRILA GELPPPTGSP
TQDGCWEVMT GGIIPSEAFD AVIKVEDVLP SDSTSDSLGR LLVGFTTPVK SGQHFRRQGE
QFHAGDLLLR AGEVIAPEHV MLLAAAGITS VQARTSARPR REIERRVAIL TTGKEVVPFN
DFARGARIET GQVIDCITPF LQATLLSRGC EPVLLASAGD SATALRASLD AALESGSFDL
IITVAGVSLG SADHTPAVLA SLGLEEIFHG VAIRPGGPVM LSRHRASDTP VLSLPGNPMA
SAVCLQSFGA AILDGSSPYA GGEGWSELDL GHFSEEEEEE QNASWQDWLE RLKPGMSTFA
ALPVSDQGMP TLRGVLSAGR RTGPCALGSL IGAGAWVRAD RAASRGGKDK VFWRPF
//
