ID A0A0D1DMR1_USTMA Unreviewed; 682 AA.
AC A0A0D1DMR1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=MoaB/Mog domain-containing protein {ECO:0000259|SMART:SM00852};
GN ORFNames=UMAG_12327 {ECO:0000313|EMBL:KIS65819.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS65819.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS65819.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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}.
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DR EMBL; CM003161; KIS65819.1; -; Genomic_DNA.
DR RefSeq; XP_011392644.1; XM_011394342.1.
DR AlphaFoldDB; A0A0D1DMR1; -.
DR STRING; 237631.A0A0D1DMR1; -.
DR EnsemblFungi; KIS65819; KIS65819; UMAG_12327.
DR GeneID; 23568072; -.
DR KEGG; uma:UMAG_12327; -.
DR VEuPathDB; FungiDB:UMAG_12327; -.
DR eggNOG; KOG2371; Eukaryota.
DR InParanoid; A0A0D1DMR1; -.
DR OrthoDB; 275356at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000561; Chromosome 22.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
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:UP000000561};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 7..156
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 437..584
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 166..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 71471 MW; AB4F8B11E6ED03E6 CRC64;
MHLYRAGILT VSDTASADAS LDRSGAVLSE QLVTAGFRDV QRRICPDNVD AIRGQVQSLV
DDEHVQLVIT TGGTGFGLRD VTPEAVEPLI TRKTPALTHA LTAHSLTKTP LAALSRGITG
IRKCASDKEA LIVCLPGSPK AVKECLQVLL GNGLLKHALE LLAGGSGEPR HKQMQGGLHR
TSAATANAAA AAVDTSTETG CAHHHHHHHH HHGGSGLHSH SAPKPRTTPL DHSAFRTVDP
SSGASLRHRT SPYPLLHLDE ALSLIAQHTP SPTTIETLAL STQLIGHVLA EDVKATCDLP
PGATTNVDGY AVKASATPPG VYEVITLQAL QSGSALEAGK ILRINTGQGL PAATDSVVMV
EDTELNSSHV ETGEELTVRI LAQVEQGENV RARGSDVEAG QVVLRKGTTI SALGGEIGTL
AFLGRSEVKV YRKPTIAILS TGNELIDPAR APTAASTTTE WGFNVFDANR PGLHAAIRAL
GFEIVDLGIS SDSVDSTLAA LTRGLGEADV ILTTGGTSMG EADLLKPLIE RQLKGTIHFG
RVAIKPGKPT TFATVEDKII FALPGNPASA LVTFYVFVLP CLRKWCGFAP NDDAVNAWNL
PKVAVTLAAE MRLDARPEFH RVVVKAEHAA LVAYSTGSQR SSGMHSMSTA NALIALPALQ
PGAPSVLPKG SQAHAILLGT IV
//
