ID   A0A177DFV5_ALTAL        Unreviewed;       672 AA.
AC   A0A177DFV5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   RecName: Full=cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575};
DE            EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575};
GN   ORFNames=CC77DRAFT_204247 {ECO:0000313|EMBL:OAG18653.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG18653.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG18653.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG18653.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046}.
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DR   EMBL; KV441483; OAG18653.1; -; Genomic_DNA.
DR   RefSeq; XP_018384074.1; XM_018530620.1.
DR   AlphaFoldDB; A0A177DFV5; -.
DR   STRING; 5599.A0A177DFV5; -.
DR   GeneID; 29116214; -.
DR   KEGG; aalt:CC77DRAFT_204247; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_204247; -.
DR   OMA; DMEHEPL; -.
DR   OrthoDB; 9838at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01420; MoaC_PE; 1.
DR   Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR   InterPro; IPR047594; MoaC_bact/euk.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT   DOMAIN          498..657
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   REGION          215..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          23..119
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        412..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..481
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   672 AA;  74798 MW;  78CA35922EED7FD9 CRC64;
     MDLHSIRDFL AEVKLPQGSD RTIQILETNI INLQDRIARV VHQIDRPATN VKEAKEKERL
     EAQRFEYEEL LGETVEKYTS RFAALRRQAK LRKQKEEILE KKRALVKQLE EQEEAERRAR
     MVVRAREEGK ERDGKSLGDI LDDALKKIRK EPTHPPKIQE QRDRKVLPSD WVVRSVGGSG
     PYSVLGRNEL DRSSEENALA DPIMDKGRVP TVPGEGHAFD LLSSSPSSSP SKRPGLVVPP
     SGILPIDEDL IVTFDAPVPQ LQQQVLALRD RLKKSYPRLD VLPYEVWTSE NKRTLQTWLK
     ILIERWQARF ENVNLTGQMV KGIVDEKLKA VLDQMVIDHN LDNDAAERMA MRWHDVSSER
     QSLTGDAEGK LDWDEMEAEG LGFLADDMEH EPLQQQQPDV EAVAQAQHGM TEVVRGESSG
     STTSRLVGRR MYSTSSRYAT FPSPEAESKP SSIDKTDGKD KLHQRQPQTP QPPPTSEAQP
     TSPQPHLPHL TASGSAHMVS VSNKQHTTRT AIAVGTVYFT NPTPLQLIRS NSLEKGDVLG
     TSRIAGIMAA KKCPEIIPLC HPIALTHVGV ELRAFGSNSG GSSPDSLPSI PISPYSIDPG
     YGGIQIEAKV QCTGPTGVEM EALTAVMGAA LSVVDMCKAV DKFQRVQDLR VVLKEGGKSG
     VWREEGWESW QD
//