ID D2NP47_ROTMD Unreviewed; 747 AA.
AC D2NP47;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Sialic acid synthase {ECO:0000313|EMBL:BAI65415.1};
GN OrderedLocusNames=RMDY18_15830 {ECO:0000313|EMBL:BAI65415.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI65415.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI65415.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI65415.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI65415.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI65415.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
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DR EMBL; AP011540; BAI65415.1; -; Genomic_DNA.
DR RefSeq; WP_005508905.1; NC_013715.1.
DR AlphaFoldDB; D2NP47; -.
DR STRING; 680646.RMDY18_15830; -.
DR GeneID; 61436828; -.
DR KEGG; rmu:RMDY18_15830; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1082; Bacteria.
DR eggNOG; COG2089; Bacteria.
DR HOGENOM; CLU_371249_0_0_11; -.
DR Proteomes; UP000001883; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR CDD; cd17773; CBS_pair_NeuB; 1.
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 Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR036732; AFP_Neu5c_C_sf.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR42966:SF3; BLR5971 PROTEIN; 1.
DR PANTHER; PTHR42966; N-ACETYLNEURAMINATE SYNTHASE; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR Pfam; PF00571; CBS; 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 SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
DR PROSITE; PS51371; CBS; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT DOMAIN 3..62
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 404..462
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 747 AA; 82960 MW; FA40D4537CF34BBD CRC64;
MIIERNIAPY VVFAEDPILN ALQKISANGQ RIIFLVNESG ILRGSLSDGD FRRWLIANPT
ASLETSALDA ANTNPQTAPA DADPETLRAY FAKGINHVPL TDERGHLVAL AMDEQDVLRI
GKHTISEDSP SFIIAEIGNN HQGSVDFAKE LVDLAVESGA DAVKFQLRDM DALYRQRGAA
TAGEDLGVQY TLDLLSRFSL TVDQMYEVFD HVKQHDMDIM CTPWDAPSVQ ALVDYGIQGM
KIASADLTNH ELLRDVASRG LPMLVSTGMS REEEIRESVA LLRNAGASYA LLQCQSAYPA
PFKDVNLAYM DRLAEIGQCL VGYSGHERGY HVPIAAVARG AKIIEKHFTT DKTLEGNDHT
VSLLPEEFKA MVQQIREVEA AIGSAAPREV STGELMNRVN LAKSLVATRH IAKGEVVTEA
DVAVKSPGRG LQPNYLPQLL GRTMQRDVEE GSFFFEGDLK DDLVTRRDFK FDRPWGLPVR
YHDYKPLIEE AKPDFLEFHF SYKDLEINID DVFDSKLDMG FTTHLPDLFA GDFLVDLASK
DPEVWERSIA EVQRTIDITR DLTRYFTVDE DPVMVVTMGG FTKDKHIPAS ARAEKYERIG
EALKRLDASG VRLAAQTLPP YPWLMGGQQY HNLFLDPKDT AEFSRAFDTA LCLDISHTML
ACNFLNIPLS EAVEQLAPLS IHLHLVDGTG VDGEGVQVGE GDVDWASLGK QLRELAPKAS
FIPEIWQGHI NNGEGFFTAL DRLEKWL
//
