GenomeNet

Database: UniProt
Entry: N1JAB1_BLUG1
LinkDB: N1JAB1_BLUG1
Original site: N1JAB1_BLUG1 
ID   N1JAB1_BLUG1            Unreviewed;       653 AA.
AC   N1JAB1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   SubName: Full=Molybdenum cofactor biosynthesis protein {ECO:0000313|EMBL:CCU74708.1};
GN   ORFNames=BGHDH14_bgh06529 {ECO:0000313|EMBL:CCU74708.1};
OS   Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS   (Oidium monilioides f. sp. hordei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX   NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU74708.1, ECO:0000313|Proteomes:UP000015441};
RN   [1] {ECO:0000313|EMBL:CCU74708.1, ECO:0000313|Proteomes:UP000015441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH14 {ECO:0000313|EMBL:CCU74708.1};
RX   PubMed=21148392; DOI=10.1126/science.1194573;
RA   Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA   Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA   Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA   Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA   Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA   Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA   Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA   Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA   Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA   Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA   Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA   Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT   "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT   extreme parasitism.";
RL   Science 330:1543-1546(2010).
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:CCU74708.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAUH01000544; CCU74708.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1JAB1; -.
DR   STRING; 546991.N1JAB1; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   InParanoid; N1JAB1; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000015441; 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; 2.
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:UP000015441};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          6..154
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          408..558
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   653 AA;  70280 MW;  003F8BAABDFB41BF CRC64;
     MTLRAAIIII SSTAARNQSK DLSESVLREV FRKQGVGAWE VVHVGIVRDD IQDIQQTIRS
     LTDVQSSPNL IVTTGGTGFS VDDVTPEAVG PLLDKHAPGI VHGVLAAGYS ITPFALVSRP
     IAGVRNKTVI ITLPGSTKGA KESLESIIKL LPHVCQQASG ADSRTLHVGG VESLEREADF
     PFPKPYQHSL RQRKIASRIF RTNNPNLDPT HRYRSSPYPM ISVTEALEFI RTHSLSPRKI
     NISVDSNITG YVIAEDVMAT ESVPAYRASI VDGYAVIAPR DGKSSKGVFA VTSVLKPTSN
     GSAEVQTGQI ARVTTGAPLP IGATAVVMVE DTVLLSTTGS IQNEEKEVEI LVEGVREGDN
     IREIGSDIQK GDIILRNGTE ISRTGGELSL LASVGRAEVF VYQRPLVGVL STGDELVEHN
     LLGDLRPGEV RDCNRTAIIS AISGWGYSVL DLGIARDKPD KLEQMLRDAL RKVDIIVTSG
     GVSMGEHDLL KPIIERSLGG TIHFGRVSMK PGKPTTFATI PAQAETGKWT QKLIFSLPGN
     PVSALVALHL FILPSLHHTS GMLSVGLPTV MVTLDHDFSL DPERPEFHRV IVVAGKDGLL
     HASSTGEQRS SRVASLRSSN ALLCLPMGNH TLTKGDKTDA LLLSRIYSYV DNY
//
DBGET integrated database retrieval system