ID A0A0F0I8D8_ASPPU Unreviewed; 1307 AA.
AC A0A0F0I8D8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN ORFNames=P875_00034198 {ECO:0000313|EMBL:KJK62932.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK62932.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK62932.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC EC=4.6.1.17; Evidence={ECO:0000256|ARBA:ARBA00001637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-
CC methionine; Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:131766; EC=4.1.99.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000034};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoaC family.
CC {ECO:0000256|ARBA:ARBA00008484}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. MoaA family. {ECO:0000256|ARBA:ARBA00009862}.
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:KJK62932.1}.
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DR EMBL; JZEE01000589; KJK62932.1; -; Genomic_DNA.
DR STRING; 1403190.A0A0F0I8D8; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01420; MoaC_PE; 1.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21117; Twitch_MoaA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01225_B; MoaA_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR003445; Cat_transpt.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR004773; K/Na_transp_Trk/HKT.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR010505; MoaA_twitch.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00934; 2a38euk; 1.
DR NCBIfam; TIGR02666; moaA; 1.
DR NCBIfam; TIGR00581; moaC; 1.
DR PANTHER; PTHR31064; POTASSIUM TRANSPORT PROTEIN DDB_G0292412-RELATED; 1.
DR PANTHER; PTHR31064:SF37; TRANSPORTER, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF02386; TrkH; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDG01386; main_SPASM_domain-containing; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 701..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 970..994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1097..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..319
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 22..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1307 AA; 144954 MW; 765C4E14A942EC61 CRC64;
MTGFLVSRRG LTASLPSLRR YPRTYLRQKG SGRNKAASQY STASSPTENG KNDTKPLPAT
YFPNSETSTQ KPSPRWTALK TAKPFSDFLT DTFNRQHDYL RISITERCNL RCVYCMPEEG
IELSPPARLL TSPEIVYLSS LFVSQGVTKI RLTGGEPTVR KDIVPLMQSI GDLRRNGLRE
LCLTTNGISL HRKLEPMVEA GLTGVNLSLD TLDPFQFQIM TRRKGFDAVM KSIDKILELN
KMGAGIKLKV NCVVMRGVND REIIPFVEMG RDSPIEVRFI EYMPFDGNRW NQKKMLSYQE
MLAVIREKYP TLEKVVDHKN DTSKTYRVPG FQGRVGFITS MTHNFCGTCN RLRITSDGNL
KVCLFGNAEV SLRDTIRKAN NGEPIDEATM NKLQLLEAAD KAARINEEGG LVDERERELL
DIIGMAVKRK KAKHAGMGKL ENMKNRPMIL IGGNVSSETE PSDLKCQGTA TSLAMDSDPD
LPHLNTSQNV HMTKISQKAV TERSATATCL VRFSKSRPWE LLREGRGTRK GDVFSVARIA
GIMAAKQTPD IIPLCHPGIG ITGVEVDVTL VDPLPSPNDT DPSLNYGAMC VMATVSCLGR
TGVEMEAMTA TMGAALTVYD MLKAVDKGMV VDGVKLLEKK GGKSGHWIRE EQVNPIVIFW
GVSNPLRSVS YADALFMCVS AITGAGLNTV DLSSLNTFQQ AILFALLISG HAILISITVL
FVRKRAFESK FKGISNKLAQ DRESRPTSDL NAPLDVADFK VVNARPSNMD AGHGDKAPGV
TEVSPVENST DLTSDDHIHW AEDDQITIGA RRRSHHQNHR VFPMVGVGAR PDLNNHPKDA
IPNLPLREES DISRLKGMIQ GTQKYFASRG FISRNSQFYG LTPDERERLG GVEYKAVSFL
AVIVAVYWLM FLIIGMIGVG GWLEANHPDI SRENGLSPFW TGAFFAVSAF VNSGMSLLDA
NMTALQKNVY PLLTMGLLIL AGNTLYPCFL RFIIWSMRCM IPDLPAWKTW EVTLDFILDH
PRRVYTNLFP RRHTWYLLGT IIVLNAIDWA GFEILAIGNT EIEQLPPGYR VLDGLFQALA
VRSGGFYVVT ISGLRQGLLV LYVLMMYVSA FPVLVTMRNT NVYEERSLGI YAHDDPESES
EGQANPGLFM SLVRHHLLGR QDVPTAEASR SYFVHQQLRS QLSHDIWWIA LAVLFISIAE
SPNFNRDPVS YSTFNIIFEV VSAYGCVGVS VGIPGRNSSF CGGWHTISKL ILAAVALRGR
HRGLPVAIDQ AVMLPNDSLA WAEEEDAALR REKTRAWGAD KMPVGAV
//
