ID G4UIA7_NEUT9 Unreviewed; 714 AA.
AC G4UIA7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=MoaB/Mog domain-containing protein {ECO:0000259|SMART:SM00852};
GN ORFNames=NEUTE2DRAFT_85837 {ECO:0000313|EMBL:EGZ73087.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ73087.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ73087.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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|ARBA:ARBA00005046, 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}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; GL891217; EGZ73087.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UIA7; -.
DR STRING; 510952.G4UIA7; -.
DR eggNOG; KOG2371; Eukaryota.
DR HOGENOM; CLU_010186_2_2_1; -.
DR OMA; RHRESPY; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000008513; 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 CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
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; IPR008284; MoCF_biosynth_CS.
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; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
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; 2.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 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:UP000008513};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..714
FT /note="MoaB/Mog domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003469507"
FT DOMAIN 13..169
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 472..622
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 189..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 74838 MW; 4FF85DE83A222807 CRC64;
MSSSTTPVAL KAAILIVSTT AAQDPATDSA DVTLRQVFDE QQAQWEVHES KIVPDDVVQI
QKQIIHWTNQ ATAANGDNNT NTINLIVTTG GTGFAVSDQT PEAVSALLHK NAPGLVHGML
AASLQVTPFA MMSRPVAGVR NGTVIITLPG SPKGAKENLQ AVIKMLPHAC MQAAGANSRA
LHKGGVKKLE QEAGVEGGGG RGHGHGQGHG HGHKHHDHGE HRGGEGGCGA HGHGHKHGHA
GLVRHTTPSE NPKSNDPSLG PSRRHRESPY PMLSVSEALS QIAQHTPIPQ IVTSKVDSSL
IGAVLAQDVL ARENVPAFRA SIVDGYAVVV PQDGNMRGVF PVVSVSHAAP GDGENMPTLK
EGEIARITTG APLPPGATSV IMVEDTVLVS TTTSKTEDAE DGKGVEEEKE VEILAADKVR
EGENVREVGS DIKQGQLILG KGDQVSAVGG EIGLLAAVGV GEVQVYRRPV VGVLSTGDEI
VDHDRPGDLR LGEVRDTNRP TLISAARDWG YEVIDLGVAR DKAGTLEETL RQALRQVDVV
ITTGGVSMGE LDLLKPTIER SLGGTIHFGR VAMKPGKPTT FATVPVKDND GERVSKVIFS
LPGNPASALV TFHLFVLPSL HQMSGVSPPG LPKVPVTLGH DFSLDRSRPE YHRAIVSVSR
DGVLTAVSTG GQRSSRVGSM KGANALLCMP CGPEPLRKGA KVEALLMGGL RSDV
//