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Database: UniProt
Entry: A0A0A2VYV6_BEABA
LinkDB: A0A0A2VYV6_BEABA
Original site: A0A0A2VYV6_BEABA 
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
//
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