ID A0A1I3V940_9PSEU Unreviewed; 396 AA.
AC A0A1I3V940;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000256|ARBA:ARBA00020092};
DE EC=2.7.7.43 {ECO:0000256|ARBA:ARBA00012491};
DE EC=3.1.3.45 {ECO:0000256|ARBA:ARBA00013066};
DE AltName: Full=KDO 8-P phosphatase {ECO:0000256|ARBA:ARBA00031051};
GN ORFNames=SAMN05421835_110193 {ECO:0000313|EMBL:SFJ91509.1};
OS Amycolatopsis sacchari.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=115433 {ECO:0000313|EMBL:SFJ91509.1, ECO:0000313|Proteomes:UP000199025};
RN [1] {ECO:0000313|EMBL:SFJ91509.1, ECO:0000313|Proteomes:UP000199025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44468 {ECO:0000313|EMBL:SFJ91509.1,
RC ECO:0000313|Proteomes:UP000199025};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-
CC deoxy-alpha-D-manno-oct-2-ulosonate + phosphate;
CC Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45;
CC Evidence={ECO:0000256|ARBA:ARBA00000898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate +
CC diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43;
CC Evidence={ECO:0000256|ARBA:ARBA00001862};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC {ECO:0000256|ARBA:ARBA00005141}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family.
CC {ECO:0000256|ARBA:ARBA00010726}.
CC -!- SIMILARITY: Belongs to the KdsC family.
CC {ECO:0000256|ARBA:ARBA00005893}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FORP01000010; SFJ91509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3V940; -.
DR STRING; 115433.SAMN05421835_110193; -.
DR OrthoDB; 9814210at2; -.
DR UniPathway; UPA00628; -.
DR Proteomes; UP000199025; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02513; CMP-NeuAc_Synthase; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR010023; KdsC_fam.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR21485:SF5; 3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE PHOSPHATASE KDSC; 1.
DR PANTHER; PTHR21485; HAD SUPERFAMILY MEMBERS CMAS AND KDSC; 1.
DR Pfam; PF02348; CTP_transf_3; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR SFLD; SFLDG01138; C1.6.2:_Deoxy-d-mannose-octulo; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW Nucleotidyltransferase {ECO:0000313|EMBL:SFJ91509.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199025};
KW Transferase {ECO:0000313|EMBL:SFJ91509.1}.
SQ SEQUENCE 396 AA; 41692 MW; 3B932844158FD34A CRC64;
MSQLDSARVL AVVPARGGSK GVPGKNLIEV GDEPLITRAV RALGRASRVD DIVVSTDSAE
IGAVAADAGA TVFPRPAELS GDSVSSEAVL LHCLDIFRGQ HGSDPDVVLM VQCTSPFIAA
ETIDGVVSSI LDEGWDCAFT AARVHEFLWR RDGSGAAVAV NHSAEVRPLR QEREPEFRET
GAVYGMRTTG FRAAKHRFFG RIGLVEMPAS HAVEIDSHDD LAIARALAAG FDSSLGTDVD
VDAVVTDFDG VHTDDRAIVL QDGTEGVVVS RSDGAGVARL LAAGIPLMIL SVEQNPVVAA
RAKKLGAQVL HGVGDKAAVL KSWLAEQRLD PARVAYVGND LRDLDAMALV GWPVAVGDAH
PAVRQAARLV LTKVGGAGAV RELSDLVLRA YERRNA
//
