ISPD_BOVIN
ID ISPD_BOVIN Reviewed; 445 AA.
AC E1BCH6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=D-ribitol-5-phosphate cytidylyltransferase {ECO:0000250|UniProtKB:A4D126};
DE EC=2.7.7.40 {ECO:0000250|UniProtKB:A4D126};
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein {ECO:0000250|UniProtKB:A4D126};
DE AltName: Full=Isoprenoid synthase domain-containing protein {ECO:0000250|UniProtKB:A4D126};
GN Name=CRPPA; Synonyms=ISPD {ECO:0000250|UniProtKB:A4D126};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Cytidylyltransferase required for protein O-linked
CC mannosylation (By similarity). Catalyzes the formation of CDP-ribitol
CC nucleotide sugar from D-ribitol 5-phosphate (By similarity). CDP-
CC ribitol is a substrate of FKTN during the biosynthesis of the
CC phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-
CC N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate
CC structure present in alpha-dystroglycan (DAG1), which is required for
CC binding laminin G-like domain-containing extracellular proteins with
CC high affinity (By similarity). Shows activity toward other pentose
CC phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose
CC using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively.
CC Not involved in dolichol production (By similarity).
CC {ECO:0000250|UniProtKB:A4D126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol +
CC diphosphate; Xref=Rhea:RHEA:12456, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57608,
CC ChEBI:CHEBI:57695; EC=2.7.7.40;
CC Evidence={ECO:0000250|UniProtKB:A4D126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + D-ribose 5-phosphate + H(+) = CDP-D-ribose +
CC diphosphate; Xref=Rhea:RHEA:53872, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:137525; Evidence={ECO:0000250|UniProtKB:A4D126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + D-ribulose 5-phosphate + H(+) = CDP-D-ribulose +
CC diphosphate; Xref=Rhea:RHEA:53612, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58121,
CC ChEBI:CHEBI:137524; Evidence={ECO:0000250|UniProtKB:A4D126};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:A4D126}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A4D126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A4D126}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000305}.
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DR EMBL; DAAA02010006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02010023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002686725.1; XM_002686679.5.
DR RefSeq; XP_015318432.1; XM_015462946.1.
DR AlphaFoldDB; E1BCH6; -.
DR SMR; E1BCH6; -.
DR STRING; 9913.ENSBTAP00000020061; -.
DR PaxDb; E1BCH6; -.
DR PRIDE; E1BCH6; -.
DR GeneID; 104968457; -.
DR KEGG; bta:104968457; -.
DR CTD; 729920; -.
DR eggNOG; ENOG502QUUE; Eukaryota.
DR HOGENOM; CLU_033636_0_0_1; -.
DR InParanoid; E1BCH6; -.
DR OrthoDB; 1356473at2759; -.
DR TreeFam; TF328415; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070567; F:cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR040635; ISPD_C.
DR InterPro; IPR018294; ISPD_synthase_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF18706; ISPD_C; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS01295; ISPD; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..445
FT /note="D-ribitol-5-phosphate cytidylyltransferase"
FT /id="PRO_0000418386"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 59
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 66
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 205
FT /note="Positions substrate for the nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 263
FT /note="Positions substrate for the nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
SQ SEQUENCE 445 AA; 49510 MW; 6541A0C4FF8BBDD7 CRC64;
MELGPPGGSG PAEPGPRLRG LRGADAAASA SSLSRFGAEA GCRASAVAAV LPAGGSGERM
GVPTPKQFCP ILERPLISYT LQALERVSWI KDIIVAVTRE NMETMKGIIQ RYQHKRISLV
EAGVTRHRSI FNGLKALAED QPNCRLSKPE VVIIHDAVRP FVEEDVLLKV VTAAQEHGAS
GAIRPLVSTV ISPSADSCLD HSLERARYRA SEMPQAFLFD VIYDAYQQCS DYDLEFGTEC
LHLALKYSHI KAKLVEGSPD LWKVTYKRDL YAAESIIKER ISQKVCVVMD TKEDEEHVGH
CLEEMLKTEL NHVKVTSGQD LQQIILEQCY NFVCVNVMTS DFEETQRLLN MVEESNLSIL
YPVVVISVHF LDYESVPLGQ KMEKVMQIRE FAKEAKKRNI LLSGLLIYFP QEEQKLRESL
RQGTTIISAL IKERNSGLIG QLLVA
