GenomeNet

Database: UniProt
Entry: W9VLB6_9EURO
LinkDB: W9VLB6_9EURO
Original site: W9VLB6_9EURO 
ID   W9VLB6_9EURO            Unreviewed;       717 AA.
AC   W9VLB6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Molybdopterin molybdotransferase {ECO:0000313|EMBL:EXJ56313.1};
GN   ORFNames=A1O5_12580 {ECO:0000313|EMBL:EXJ56313.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ56313.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ56313.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ56313.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) 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|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}.
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:EXJ56313.1}.
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DR   EMBL; AMGX01000035; EXJ56313.1; -; Genomic_DNA.
DR   RefSeq; XP_007751339.1; XM_007753149.1.
DR   AlphaFoldDB; W9VLB6; -.
DR   STRING; 1182543.W9VLB6; -.
DR   GeneID; 19197266; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000019471; 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:UP000019471};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:EXJ56313.1}.
FT   DOMAIN          10..164
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          464..624
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          210..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   717 AA;  76001 MW;  4A535996201B529F CRC64;
     MTSPPLLRPA ILVVSDTAAA DPSTDKSIPI LKDVFSQDGA GKWSDPLVEI VKDDVLEIQR
     IVRAWTDSEN ETTNAGVVNL VVTTGGTGFA RRDFTPEAIA PLIHRHAPGI VHGMLAASFQ
     ITPFAMMSRP VAGTRNKSII ITLPGSPKGA KENLQAVLKL LPHACLQAAG QDSRAAHVGG
     VKKLEKEAGV GPSGSGDATP ATLVVGATND HSHQHSHHHS HDHDHSHEGG GSVHGGHRIP
     KAHTAPSERP QLQSNDPRLG ATARYRSSPY PMLNVSDAVA KIFENAPAST VEIRDVSPDL
     VGYVAAEDIR AAEAVPAYRA SIVDGYAVII PNKEAISQKS IKGIFPVASV SHAQASSLPP
     PLEKGQIARI TTGAPLPENA NAVVMVEDTV ISTLTPDGKE EASVEILTDE LVAGENVRES
     GSDIELGQVI VAKGTQISPL GGEIGVLAAA GIKKVPVYRK PRIGVMSTGD EVMDVAYKGT
     LSGGMIRDSN RPSLLTLLRG WRICEDVVDL GVARDTPHHE LEHKLRDAFR LHGLDIVITT
     GGVSMGELDL LKPTIERALG GTVHFGRVNM KPGKPTTFAT VPIKDSHPDS DSSRRETRLI
     FGLPGNPASA LVTANLFVLP CIQRMTGLPD PQGAPRVKVR LHGRVRCDKA RVEYHRVLVS
     ADPNDGKLVA RSTGMQRSSR VGSLASANGL LVLPQREGYI EDGGECEALI VGMVLGY
//
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