(data stored in SCRATCH zone)

SWISSPROT: D6XY17_BACIE

ID   D6XY17_BACIE            Unreviewed;       162 AA.
AC   D6XY17;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000256|HAMAP-Rule:MF_01224};
DE            EC=4.6.1.17 {ECO:0000256|HAMAP-Rule:MF_01224};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_01224};
GN   Name=moaC {ECO:0000256|HAMAP-Rule:MF_01224};
GN   OrderedLocusNames=Bsel_0554 {ECO:0000313|EMBL:ADH98090.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98090.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98090.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate to cyclic pyranopterin
CC       monophosphate (cPMP). {ECO:0000256|HAMAP-Rule:MF_01224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate =
CC         cyclic pyranopterin phosphate + diphosphate;
CC         Xref=Rhea:RHEA:49580, ChEBI:CHEBI:33019, ChEBI:CHEBI:59648,
CC         ChEBI:CHEBI:131766; EC=4.6.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01224, ECO:0000256|SAAS:SAAS01115723};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01224, ECO:0000256|SAAS:SAAS00100831}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_01224}.
CC   -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01224}.
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DR   EMBL; CP001791; ADH98090.1; -; Genomic_DNA.
DR   RefSeq; WP_013171519.1; NC_014219.1.
DR   STRING; 439292.Bsel_0554; -.
DR   EnsemblBacteria; ADH98090; ADH98090; Bsel_0554.
DR   KEGG; bse:Bsel_0554; -.
DR   eggNOG; ENOG4108YXW; Bacteria.
DR   eggNOG; COG0315; LUCA.
DR   HOGENOM; HOG000228417; -.
DR   KO; K03637; -.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 1595361at2; -.
DR   BioCyc; BSEL439292:G1GLR-595-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01420; MoaC_PE; 1.
DR   Gene3D; 3.30.70.640; -; 1.
DR   HAMAP; MF_01224_B; MoaC_B; 1.
DR   InterPro; IPR023045; Mo_CF_biosynth-C.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; SSF55040; 1.
DR   TIGRFAMs; TIGR00581; moaC; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XY17.
DR   SWISS-2DPAGE; D6XY17.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01224,
KW   ECO:0000256|SAAS:SAAS00703322};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01224,
KW   ECO:0000256|SAAS:SAAS00100825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN       15    152       MoaC. {ECO:0000259|Pfam:PF01967}.
FT   REGION       75     77       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   REGION      115    116       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   ACT_SITE    130    130       {ECO:0000256|HAMAP-Rule:MF_01224}.
SQ   SEQUENCE   162 AA;  17439 MW;  8E4A20D0A01F6ED6 CRC64;
     MESFTHFNEQ GRAKMVDISD KEETVRTAVA KSSVLVNKQI YEGIQSGHMK KGDVLAVAQV
     AGVMAAKNTA QLIPMCHPLS LSGVDIAFDW KEEGSSHRLH IRVAVKTKGS TGVEMEALTS
     ASATALTVYD MCKAVDKGMV IGETYLEEKT GGKSGDFKRA SE
//

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