ID A0A0A2VYV6_BEABA Unreviewed; 784 AA.
AC A0A0A2VYV6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000313|EMBL:KGQ11350.1};
GN ORFNames=BBAD15_g2946 {ECO:0000313|EMBL:KGQ11350.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ11350.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ11350.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ11350.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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 -!- 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:KGQ11350.1}.
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DR EMBL; ANFO01000226; KGQ11350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VYV6; -.
DR STRING; 1245745.A0A0A2VYV6; -.
DR HOGENOM; CLU_009273_7_2_1; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
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:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01420; MoaC_PE; 1.
DR CDD; cd00756; MoaE; 1.
DR CDD; cd00886; MogA_MoaB; 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; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 3.90.1170.40; Molybdopterin biosynthesis MoaE subunit; 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; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR010505; MoaA_twitch.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02666; moaA; 1.
DR NCBIfam; TIGR00581; moaC; 1.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR22960:SF28; GTP 3',8-CYCLASE; 1.
DR PANTHER; PTHR22960; MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF02391; MoaE; 1.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDG01216; thioether_bond_formation_requi; 1.
DR SMART; SM00729; Elp3; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR SUPFAM; SSF54690; Molybdopterin synthase subunit MoaE; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 19..245
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 784 AA; 87056 MW; 8E730D14C8076C44 CRC64;
MTASPVFGKV YSVSQLTDAF ARKFYYLRLS ITDVCNFRCS YCLPDGYKPH GVANKSFLNV
DEIRRITRAF AALGTEKVRL TGGEPSLRRD FTEIIAAVRE NASIRQLAVT TNGYRLARDV
NAWRDAGLTA LNVSVDSLDA RQFHAITGQD KFRQVMEGID AAFSVGFERV KVNTVLMRDV
NHNQLETFLA WIKPRPIQLR FIELMETGDG GTLFRKHHIS GKTIRDQLLE RGWVHQLRQR
SDGPAQVFCH PDYKGEIGLI MPYEKDFCAS CNRLRVSSIG NLHLCLFGEQ GIALRDLLAD
DAQQSELEGR ISSALAQKKQ THFLHDGNTG ITQNLSRRGE DDDTSGHYLS EVATEAGHQV
VDKAIVKENR YAIRAAVSQW IADEQVQVVL INGGTGFTDG DQTPEALLPL FDREVEGFGE
LFRMLSFEEI GTSTLQSRAV AGMANKTLIF AMPGSTKACR TAWENIIQPQ LDAPHMVDVS
AKAETVREAR AEAFVTMLPD TLAMIVDGSH HKGDVFATAR IAGIQAAKRT WELIPLCHPL
LLSKVEVQLE AQTEHSRVRI ESVCRLTGKT GVEMEALTAA SVAALTIYDM CKAVQKDMVI
GPVRELVGCD SLTLDEAYGD VEQLRAALAD KGSRWALALE SGKLLAAVNQ TLYQWLSQCD
EDGAVVTFTG KVRNHNLGDS VSALTLEHYP GMTEKALAEI VAEARSRWPL QRVTVIHRIG
ELWPGDEIVF VGVTGAHRSS AFEAAQFIMD YLKTRAPFWK REATAEGDRW VEARDSDKQA
AKRW
//