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Database: UniProt
Entry: A0A151MQQ7_ALLMI
LinkDB: A0A151MQQ7_ALLMI
Original site: A0A151MQQ7_ALLMI 
ID   A0A151MQQ7_ALLMI        Unreviewed;       417 AA.
AC   A0A151MQQ7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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};
GN   Name=ISPD {ECO:0000313|EMBL:KYO26749.1};
GN   ORFNames=Y1Q_0019212 {ECO:0000313|EMBL:KYO26749.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO26749.1};
RN   [1] {ECO:0000313|EMBL:KYO26749.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO26749.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO26749.1}.
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DR   EMBL; AKHW03005461; KYO26749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151MQQ7; -.
DR   STRING; 8496.A0A151MQQ7; -.
DR   eggNOG; ENOG502QUUE; Eukaryota.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000050525; 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:UP000050525}.
FT   DOMAIN          249..395
FT                   /note="D-ribitol-5-phosphate cytidylyltransferase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18706"
SQ   SEQUENCE   417 AA;  46579 MW;  D09DB1ABD595527B CRC64;
     MELSDSWSAG SVAAVLPAGG SGERLGAARP KQFCALQGRP LVSHTARALE RISWISDIIV
     VVSLEHIETM KSIIQKYGHK RITVVEGGVT RHRSIFNGLK IFAENKLSNC PLQKPEVVII
     HDAVRPFIEE DILLKVVKAA KDHGAAGAIR PLVSTVVASS ADGCLDHSLE RARYRASEMP
     QAFLFDIIYQ AYHQCNDYDL DYGTECLHLA LKYCKTKAKL IEGSPDLWKV TYKRDLYAAE
     SIIKDNLSQQ VCVITDMKGD DVQVGFLLHE TLKSHIKQVK RISVSLCKDD NYMQNIILGQ
     CYNFICMHVK KSAFQETQQL VDILENANVS TLYPVVLISV HLNVSENASF SSEMEDLTRI
     KEFAREVKKK NILVYGLLIH YNKDDPQLQE TVNSAATIIS ALIKDRNPEL IGQLLVA
//
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