ID A0A091UTE2_NIPNI Unreviewed; 331 AA.
AC A0A091UTE2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=Y956_03074 {ECO:0000313|EMBL:KFQ93961.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ93961.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ93961.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ93961.1};
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; KL410115; KFQ93961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UTE2; -.
DR STRING; 128390.A0A091UTE2; -.
DR eggNOG; ENOG502QUUE; Eukaryota.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053283; 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:UP000053283}.
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:KFQ93961.1"
FT NON_TER 331
FT /evidence="ECO:0000313|EMBL:KFQ93961.1"
SQ SEQUENCE 331 AA; 37463 MW; 462B4634CD8554C3 CRC64;
RISWISDIIV VVSPENIETM KSIIEKYGHK RVTIVKGGIT RHRSIFNGLK VFTENEFSNR
LLQKPEVVII HDAVRPFVEE DILSKVVMAA KEHGAAGAIR PLVSTVIASA ADGCLDHSLE
RARYRASEMP QAFLFDIIYE AYQQCTDYDL DYGTECLHLA LKYCKANARL VEGTADLWKV
TYKRDLYAAE SIIKDNLSQQ VCVITDVKEA VAQVGFLLHE SLKSQIKVEA MSISLSKNDS
HLQNIFSGQC YNFVCVNDKK YAIQETQQLV ETLEKSNIPL LYPVVLISVH LDISENISFS
IGMEELARIK KFAREVKKKN ILVYGLLIQY K
//
