ID Q9EU02_CAMJU Unreviewed; 343 AA.
AC Q9EU02;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 28-JUN-2023, entry version 64.
DE SubName: Full=Putative sialic acid synthase {ECO:0000313|EMBL:AAG37021.1};
DE SubName: Full=SiaC {ECO:0000313|EMBL:AAG29923.1};
GN Name=neuB1 {ECO:0000313|EMBL:AAG37021.1};
GN Synonyms=siaC {ECO:0000313|EMBL:AAG29923.1};
OS Campylobacter jejuni.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197 {ECO:0000313|EMBL:AAG37021.1};
RN [1] {ECO:0000313|EMBL:AAG29923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSC57360 {ECO:0000313|EMBL:AAG29923.1};
RA Guerry P., Ewing C.P., Moran A.P., Trust T.J.;
RT "Distinct Functional Alleles of Sialic Acid Biosynthetic Genes in
RT Campylobacter Species.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAG37021.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSC 57360 {ECO:0000313|EMBL:AAG37021.1};
RX PubMed=11083778; DOI=10.1128/IAI.68.12.6656-6662.2000;
RA Guerry P., Ewing C.P., Hickey T.E., Prendergast M.M., Moran A.P.;
RT "Sialylation of lipooligosaccharide cores affects immunogenicity and serum
RT resistance of Campylobacter jejuni.";
RL Infect. Immun. 68:6656-6662(2000).
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DR EMBL; AF195055; AAG29923.1; -; Genomic_DNA.
DR EMBL; AF257460; AAG37021.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EU02; -.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR CDD; cd11615; SAF_NeuB_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.90.1210.10; Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR036732; AFP_Neu5c_C_sf.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR PANTHER; PTHR42966; N-ACETYLNEURAMINATE SYNTHASE; 1.
DR PANTHER; PTHR42966:SF1; SIALIC ACID SYNTHASE; 1.
DR Pfam; PF03102; NeuB; 1.
DR Pfam; PF08666; SAF; 1.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; AFP III-like domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 4: Predicted;
FT DOMAIN 286..343
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 343 AA; 38482 MW; 659856BD98981F92 CRC64;
MQIKIDKLTI SQKNPLIIPE IGINHNGSLE IAKLMVDAAK RAGAKIIKHQ THIVEDEMSQ
EAKNVIPGNA NISIYEIMEQ CALNYKDELA LKEYVEKQGL VYLSTPFSRA AANRLEDMGV
SAYKIGSGEC NNYPLIKHIA QFKKPMIIST GMNSIESIKP TVKILRDYEI PFVLLHTTNL
YPTPSHLVRL QAMLELYKEF NCLYGLSDHT TNNLACIGAI ALGASVLERH FTESMDRKGP
DIVCSMDEST LKDLINQTQE MVLLRGDNNK NPLKEEQVTI DFAFASVVSI KDIKKGEILS
MDNIWVKRPS KGGISAKDFE AILGKRAKKD IKNNIQLTWD DFE
//
