ID C1DUB4_SULAA Unreviewed; 304 AA.
AC C1DUB4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575};
DE EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575};
GN OrderedLocusNames=SULAZ_0716 {ECO:0000313|EMBL:ACN99589.1};
OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium.
OX NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN99589.1, ECO:0000313|Proteomes:UP000001369};
RN [1] {ECO:0000313|EMBL:ACN99589.1, ECO:0000313|Proteomes:UP000001369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825
RC {ECO:0000313|Proteomes:UP000001369};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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; CP001229; ACN99589.1; -; Genomic_DNA.
DR RefSeq; WP_012674901.1; NC_012438.1.
DR AlphaFoldDB; C1DUB4; -.
DR STRING; 204536.SULAZ_0716; -.
DR KEGG; saf:SULAZ_0716; -.
DR eggNOG; COG0315; Bacteria.
DR eggNOG; COG0521; Bacteria.
DR HOGENOM; CLU_063423_1_1_0; -.
DR OrthoDB; 9794429at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001369; Chromosome.
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 CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
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; IPR012247; MoaC_MogA.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR NCBIfam; TIGR00581; moaC; 1.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDOTRANSFERASE; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF036594; MoaC_MogA; 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.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000001369}.
FT DOMAIN 150..294
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 304 AA; 33590 MW; 27DA761E53907306 CRC64;
MKMADVSMKF ETIREAQAEG KIYLSKETIE MIKNKQIPKG DVITASQMAG LLGAKKTPEV
LPFCHPILID QAFVEVQLQE DGIYVKSFVR CIGRTGVEME ALTAVSAALL NVYDMCKAFD
KNMVISDIKL VSKKGGKSDY EEDLSGLKCA VITLSDSCYR KEAEDKSGKV AIDIIENEFK
GEVVHYEILP DDKEKIVEKL KQLTDKVDII FTTGGTGFGK RDNTPEATKE VIEKEMIGFE
EAMRIIGIRF TPKSLLSRAV CGIAGDHTLI INLPGSSSGV RDNLKMIAPL LKHAIRMAKG
EKKH
//
