ID A0A137P9H9_CONC2 Unreviewed; 643 AA.
AC A0A137P9H9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=MoaB/Mog domain-containing protein {ECO:0000259|SMART:SM00852};
GN ORFNames=CONCODRAFT_81578 {ECO:0000313|EMBL:KXN71649.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN71649.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN71649.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN71649.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KQ964470; KXN71649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137P9H9; -.
DR STRING; 796925.A0A137P9H9; -.
DR EnsemblFungi; KXN71649; KXN71649; CONCODRAFT_81578.
DR OMA; ESPYPMI; -.
DR OrthoDB; 275356at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000070444; 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:UP000070444};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 6..153
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 398..544
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 69294 MW; 1E9A11CEA5A05DA6 CRC64;
MAYTVGILTI SDRTFQGTSE DKSSPKIQEF LLEKSKDLWN VTQKKVVPDE IEQIQNTILK
WTDVDKVNLI VTTGGTGWST RDTTPEAVIP LLHKRVNGIE IALISQGLNF TPLATLARPV
CGIRGNSLIV TLPGSPKACA EGLSIIYPGL SHGLSLVLGD SGNEFHSKMN KESKSQGQNA
GCHHHCPKVS SGKLPTTSGV QVAYRARESP YPMLPVKEAE NLIREQINKL PNAIVETSIT
DLKAGSVIAS EVKAQQPVPA YRASVVDGYA VRSSDGPGVY PVLSQSSLAG SQSSLQLLPG
HIMRITTGAR VPDEADAVVM VEYTKLIEAS EDGKVEIKVE ILSQMDPGNN VREIGSDISQ
GSVILKSNSI VSPFGAETVT LSTGGVDKVK IHRRPVVGVM STGGELVTLD YSEPLRPGQV
KDANRPSLLN ILSSHQYPIK DLGIVEDNPS TLTDKIYKSL EEVDVLITTG GVSMGEMDLI
KEMIQTDPKF QVHFGRIKMK PGKPATFATY HPSPEKTTLF FALPGNPVSA IVTFYLLVLP
ALRQFENHPC PQLPKLKVKL THPIKLDSRP EYLRAVVTNE ISSDGNKLKA TSLNVGKTQP
SSQTTTLAGA NALLELPAKS AELASLTEGD EVVAILINPI QYS
//
