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Database: UniProt
Entry: A0A0F0L9N7_9MICO
LinkDB: A0A0F0L9N7_9MICO
Original site: A0A0F0L9N7_9MICO 
ID   A0A0F0L9N7_9MICO        Unreviewed;       387 AA.
AC   A0A0F0L9N7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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   Name=neuA {ECO:0000313|EMBL:KJL29848.1};
GN   ORFNames=RS83_01419 {ECO:0000313|EMBL:KJL29848.1};
OS   Microbacterium oxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL29848.1, ECO:0000313|Proteomes:UP000033640};
RN   [1] {ECO:0000313|EMBL:KJL29848.1, ECO:0000313|Proteomes:UP000033640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEL4b {ECO:0000313|EMBL:KJL29848.1,
RC   ECO:0000313|Proteomes:UP000033640};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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   -!- 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:KJL29848.1}.
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DR   EMBL; JYIW01000022; KJL29848.1; -; Genomic_DNA.
DR   RefSeq; WP_045278803.1; NZ_JYIW01000022.1.
DR   AlphaFoldDB; A0A0F0L9N7; -.
DR   PATRIC; fig|82380.11.peg.1454; -.
DR   OrthoDB; 9805604at2; -.
DR   UniPathway; UPA00628; -.
DR   Proteomes; UP000033640; Unassembled WGS sequence.
DR   GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IEA:RHEA.
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; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 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:KJL29848.1};
KW   Transferase {ECO:0000313|EMBL:KJL29848.1}.
SQ   SEQUENCE   387 AA;  41565 MW;  60A7C69B380B17BC CRC64;
     MTDTTTVTAV AIIPARGGSK GVPRKNLQPV GGVPLVQRAI HAAQAAEGID LVVVSTDDAE
     IAAVSEAAGA RVVHRPAELS GDTASSESAI LHALDHLELE GVTPQIVAFL QATSPFIPSA
     ALATAVSDIR AGRADSVFSA FETYGFLWRR GADGEGIAIN HDASFRPRRQ DREPHHLESG
     AFYVFRTEGF RESRHRFFGR IRIAEVPEWT AIEIDDEQQL GIARALAARQ EQPHPIPANA
     VVTDFDGVHT DDTAIVDADG REQVRVSRED GMGVAMLRRA GVPMLILSTE VNPVVRARAE
     KLRVPVLHGI DDKESALRAW AETTGVALDD IAYLGNDVND LPAMRIVGWP VAVANAHPKV
     LEQARVILSR SGGDGAVREL IERVLSS
//
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