ID   KDSB_MAIZE              Reviewed;         298 AA.
AC   Q9M4G3; B6TZC2; K7VDG8; Q9M4D3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {ECO:0000305};
DE            EC=2.7.7.38 {ECO:0000269|PubMed:10829033};
DE   AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase {ECO:0000303|PubMed:10829033};
DE            Short=CMP-KDO synthase {ECO:0000303|PubMed:10829033};
DE            Short=ZmCKS {ECO:0000303|PubMed:10829033};
GN   Name=KDSB {ECO:0000305};
GN   Synonyms=CKS {ECO:0000303|PubMed:10829033}, KDO1 {ECO:0000305};
GN   ORFNames=GRMZM2G119256 {ECO:0000305},
GN   ZEAMMB73_836886 {ECO:0000312|EMBL:AFW81111.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Endosperm;
RX   PubMed=10829033; DOI=10.1074/jbc.m905750199;
RA   Royo J., Gomez E., Hueros G.;
RT   "A maize homologue of the bacterial CMP-3-deoxy-D-manno-2-octulosonate
RT   (KDO) synthetases. Similar pathways operate in plants and bacteria for the
RT   activation of KDO prior to its incorporation into outer cellular
RT   envelopes.";
RL   J. Biol. Chem. 275:24993-24999(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73;
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
CC   -!- FUNCTION: Catalyzes the production of the sugar nucleotide CMP-3-deoxy-
CC       D-manno-octulosonate (CMP-KDO) (PubMed:10829033). CTP is the preferred
CC       nucleotide donor, and it can partially be replaced with UTP but not
CC       with ATP (PubMed:10829033). Activates KDO during the biosynthesis of
CC       rhamnogalacturonan II (RG-II), a structurally complex pectic
CC       polysaccharide of the primary cell wall (By similarity). RG-II is
CC       essential for the cell wall integrity of rapidly growing tissues and
CC       pollen tube growth and elongation (By similarity).
CC       {ECO:0000250|UniProtKB:Q9C920, ECO:0000269|PubMed:10829033}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-
CC         beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986,
CC         ChEBI:CHEBI:85987; EC=2.7.7.38;
CC         Evidence={ECO:0000269|PubMed:10829033};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9C920};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:10829033};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-
CC       octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-
CC       deoxy-D-manno-octulosonate and CTP: step 1/1. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9M4G3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9M4G3-2; Sequence=VSP_058579, VSP_058580;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10829033}.
CC   -!- MISCELLANEOUS: Rhamnogalacturonan II (RG-II) RG-II is a structurally
CC       complex pectic polysaccharide present in the primary cell wall. RG-II
CC       consists of a linear 1,4-linked a-Dgalacturonic acid backbone with four
CC       distinct side chains, two of which contain apiosyl residues. Boric acid
CC       forms a diester with two apiosyl residues from separate RG-II
CC       molecules, thereby covalently cross-linking two RG-II molecules as a
CC       dimer. {ECO:0000250|UniProtKB:Q9C920}.
CC   -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000305}.
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DR   EMBL; AJ242474; CAB89846.1; -; mRNA.
DR   EMBL; AJ250331; CAB89847.1; -; Genomic_DNA.
DR   EMBL; CM000784; AFW81111.1; -; Genomic_DNA.
DR   EMBL; CM000784; AFW81112.1; -; Genomic_DNA.
DR   EMBL; EU970337; ACG42455.1; -; mRNA.
DR   RefSeq; NP_001105657.1; NM_001112187.1. [Q9M4G3-1]
DR   AlphaFoldDB; Q9M4G3; -.
DR   SMR; Q9M4G3; -.
DR   STRING; 4577.GRMZM2G119256_P02; -.
DR   PaxDb; Q9M4G3; -.
DR   PRIDE; Q9M4G3; -.
DR   EnsemblPlants; Zm00001eb343610_T001; Zm00001eb343610_P001; Zm00001eb343610. [Q9M4G3-1]
DR   EnsemblPlants; Zm00001eb343610_T002; Zm00001eb343610_P002; Zm00001eb343610. [Q9M4G3-2]
DR   GeneID; 542667; -.
DR   Gramene; Zm00001eb343610_T001; Zm00001eb343610_P001; Zm00001eb343610. [Q9M4G3-1]
DR   Gramene; Zm00001eb343610_T002; Zm00001eb343610_P002; Zm00001eb343610. [Q9M4G3-2]
DR   KEGG; zma:542667; -.
DR   eggNOG; ENOG502QPIP; Eukaryota.
DR   HOGENOM; CLU_065038_2_0_1; -.
DR   OMA; FMATCAK; -.
DR   BioCyc; MetaCyc:MON-11935; -.
DR   BRENDA; 2.7.7.38; 6752.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000007305; Chromosome 8.
DR   ExpressionAtlas; Q9M4G3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02517; CMP-KDO-Synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00057; KdsB; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR004528; KdsB.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00466; kdsB; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell wall biogenesis/degradation; Magnesium;
KW   Membrane; Nucleotidyltransferase; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..298
FT                   /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT                   /id="PRO_0000437957"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         269..280
FT                   /note="VIKVDHDAHGVD -> QHIFLYGDQSGP (in isoform 2)"
FT                   /id="VSP_058579"
FT   VAR_SEQ         281..298
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058580"
FT   CONFLICT        195
FT                   /note="V -> F (in Ref. 3; ACG42455)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   298 AA;  32579 MW;  483E012679BE2CB9 CRC64;
     MPICAPSSDS SASASSGLGA RVWVLHGLAL GAAAAAAAVA YLYRRPTGFR SRAVGIIPAR
     FASTRFEGKP LVPILGKPMI QRTWERVMLA SSLDHVVVAT DDERIAECCR GFGADVIMTS
     ASCKNGSERC CEALKKLDKH YDIVVNIQGD EPLIEPEIID GVVMSLQRAP DAVFSTAVTS
     LKPEDAFDTN RVKCVVDNLG YAIYFSRGLI PFNKSGNANP KYPYLLHLGI AGFDSKFLKI
     YPELPPTPLQ MEEDLEQLKV LENGYRMKVI KVDHDAHGVD APEDVEKIEA LMRTRNIQ