(data stored in ACNUC1104 zone)

SWISSPROT: A4F786_SACEN

ID   A4F786_SACEN            Unreviewed;       159 AA.
AC   A4F786;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 95.
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   ECO:0000313|EMBL:CAL99910.1};
GN   OrderedLocusNames=SACE_0564 {ECO:0000313|EMBL:CAL99910.1};
GN   ORFNames=A8924_0964 {ECO:0000313|EMBL:PFG93713.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99910.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99910.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99910.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93713.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93713.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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; AM420293; CAL99910.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93713.1; -; Genomic_DNA.
DR   RefSeq; WP_009945207.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0564; -.
DR   EnsemblBacteria; CAL99910; CAL99910; SACE_0564.
DR   KEGG; sen:SACE_0564; -.
DR   eggNOG; ENOG4108YXW; Bacteria.
DR   eggNOG; COG0315; LUCA.
DR   HOGENOM; HOG000228417; -.
DR   KO; K03637; -.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 1595361at2; -.
DR   BioCyc; SERY405948:SACE_RS02775-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F786.
DR   SWISS-2DPAGE; A4F786.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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:UP000006728}.
FT   DOMAIN       17    150       MoaC. {ECO:0000259|Pfam:PF01967}.
FT   REGION       77     79       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   REGION      113    114       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   ACT_SITE    128    128       {ECO:0000256|HAMAP-Rule:MF_01224}.
SQ   SEQUENCE   159 AA;  16561 MW;  79C4D9810D23C916 CRC64;
     MAQSDLTHVD EAGAARMVDV SGKQVTARTA VASGVLRTTA EVIGLLRRDG LPKGDALATG
     RLAGIMAAKR TPDLIPLCHP IALSGVKVDL EVGDAEVRIT ATVRTTDRTG VEMEALTAVT
     GAGLALHDMI KAVDPAAVLD AVRVERKEGG KTGTWVREE
//

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