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Database: UniProt
Entry: A1DIB3_NEOFI
LinkDB: A1DIB3_NEOFI
Original site: A1DIB3_NEOFI 
ID   A1DIB3_NEOFI            Unreviewed;       713 AA.
AC   A1DIB3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   SubName: Full=Molybdenum cofactor biosynthesis protein Gephyrin, putative {ECO:0000313|EMBL:EAW19120.1};
GN   ORFNames=NFIA_090780 {ECO:0000313|EMBL:EAW19120.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW19120.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW19120.1; -; Genomic_DNA.
DR   RefSeq; XP_001261017.1; XM_001261016.1.
DR   AlphaFoldDB; A1DIB3; -.
DR   STRING; 331117.A1DIB3; -.
DR   EnsemblFungi; EAW19120; EAW19120; NFIA_090780.
DR   GeneID; 4587575; -.
DR   KEGG; nfi:NFIA_090780; -.
DR   VEuPathDB; FungiDB:NFIA_090780; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   OMA; RHRESPY; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000006702; 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; 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:UP000006702};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          9..157
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          441..606
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          181..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..218
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  74494 MW;  6A4849A474589ED1 CRC64;
     MADGKLRAAI LVVSDTASQD PSTDKVGDTL TTSFAAEGSN SWDPPVIKIV PDNVLDIQRT
     ICNWTDGPDW FNLVLISGGT GFAVKDNTPE AVSPLIHRHA PGLVHGMLAA SLKVTPFAMM
     SRPVAGVRDK SLLIILPGSP KGAKENLEAI IKLLPHACTQ AAGANSRALH AGGVKKLEAE
     AGIASQSQSS GSKVQSHDHH HHHHHHHNHG HSHGHGHVVP RAHTSPSEWP QSNDPNAGPN
     RRYRSSPYPM LSVDDALKLI SQHTPEPVVI EVPVTPSLVG SVVAEDVYAG EAVPAYRASI
     VDGYAVIAPD SPTAERSTKG IFPVASIAHA NPGGTLSPLE PGTVARITTG APVPPNANAV
     VMVEDTVLVS STPDGQEEAT IEILTGDIKP LENVREPGSD VALGSKILSK GDLITSVGGE
     IGLLAATGTK TVKVYKKPCV GVLSTGDELV EHNDPTKLIG GQIRDSNRPS LLSCLSSWGF
     PTVDLGIARD TPPTELENAL RDALRGVGRA STSVDVIVTT GGVSMGELDL LKPTIERSLG
     GTIHFGRVSM KPGKPTTFAT IPFKPSSLPT GSAQQERESK LIFSLPGNPA SALVTLNLFV
     LPSLHKLMGM GQRQTAPGVT PALGLPLVSV TLAHPFPLDP KRTEYHRAIV TASRSDGRLY
     ATSTGLEGVG QRSSRVGSLA SANALLVLQP GSGKVDKGTL VEALLLGNVV PEA
//
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