ID A0A087R7F4_APTFO Unreviewed; 331 AA.
AC A0A087R7F4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=D-ribitol-5-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00015848};
DE EC=2.7.7.40 {ECO:0000256|ARBA:ARBA00012488};
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein {ECO:0000256|ARBA:ARBA00031950};
DE AltName: Full=Isoprenoid synthase domain-containing protein {ECO:0000256|ARBA:ARBA00032606};
DE Flags: Fragment;
GN ORFNames=AS27_03454 {ECO:0000313|EMBL:KFM09408.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM09408.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM09408.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM09408.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000831};
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:0000256|ARBA:ARBA00000413};
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:0000256|ARBA:ARBA00000888};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789}.
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DR EMBL; KL226155; KFM09408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R7F4; -.
DR STRING; 9233.A0A087R7F4; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR040635; ISPD_C.
DR InterPro; IPR018294; ISPD_synthase_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43015; D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43015:SF1; D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF18706; ISPD_C; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS01295; ISPD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT DOMAIN 199..331
FT /note="D-ribitol-5-phosphate cytidylyltransferase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18706"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM09408.1"
FT NON_TER 331
FT /evidence="ECO:0000313|EMBL:KFM09408.1"
SQ SEQUENCE 331 AA; 37528 MW; 5952470A4B2E9EF6 CRC64;
RISWISDIIV VVSPENIETM KSIIEKYGHK RVMIVKGGIT RHRSIFNGLK VFAENEFSNH
LLQKPEVVII HDAVRPFVEE DILSKVVMAA KEHGAAGAIR PLVSTVIASA ADGCLDHSLE
RARYRASEMP QAFLFDTIYE AYQQCTDYDL DYGTECLHLA LKYCNTNAKL VEGTADLWKV
TYKRDLYAAE SIIKDNLSQQ VCVITNVKEA VAQVGFLLHE SLKSQIKVEV VSISLSKNDS
YLQNIFSGQC YNFICVNDKK YAIQETQQLV DMLEKSNIPL LYPVVLILVH LDISENISFS
IGMEEITRIK KFAREVKKKN ILVYGLLIQY K
//
