(data stored in SCRATCH zone)

SWISSPROT: C7QHD0_CATAD

ID   C7QHD0_CATAD            Unreviewed;       178 AA.
AC   C7QHD0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 66.
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=Caci_0114 {ECO:0000313|EMBL:ACU69069.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69069.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69069.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-
CC       triphosphate = cyclic pyranopterin phosphate + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01224, ECO:0000256|SAAS:SAAS00703327}.
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; CP001700; ACU69069.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QHD0; -.
DR   STRING; 479433.Caci_0114; -.
DR   EnsemblBacteria; ACU69069; ACU69069; Caci_0114.
DR   KEGG; cai:Caci_0114; -.
DR   eggNOG; ENOG4108YXW; Bacteria.
DR   eggNOG; COG0315; LUCA.
DR   HOGENOM; HOG000228417; -.
DR   KO; K03637; -.
DR   OMA; MCKAIDK; -.
DR   OrthoDB; POG091H04V3; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
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; 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; C7QHD0.
DR   SWISS-2DPAGE; C7QHD0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
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:UP000000851}.
FT   DOMAIN       36    169       MoaC. {ECO:0000259|Pfam:PF01967}.
FT   REGION       96     98       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   REGION      132    133       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   ACT_SITE    147    147       {ECO:0000256|HAMAP-Rule:MF_01224}.
SQ   SEQUENCE   178 AA;  18049 MW;  67836218EC81CBE3 CRC64;
     MSSETSGTVE TSGVAEAPGG KSDRLTHIDS TGDARMVDVT AKPVSARQAR ATGFVEVSPK
     VVELLRGEGM PKGDALSVAR IAGIMGAKKT PDLVPLCHPI AISGVKVALE VEDSGVAIAA
     TVKTADRTGV EMEALTAVAV AGLTVIDMVK AVDPAAVLTR VQVEAKSGGV SGDWSREG
//

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