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Database: UniProt
Entry: G2DE65_9GAMM
LinkDB: G2DE65_9GAMM
Original site: G2DE65_9GAMM 
ID   G2DE65_9GAMM            Unreviewed;       355 AA.
AC   G2DE65;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=N-acetylneuraminate synthase {ECO:0000313|EMBL:EGV51075.1};
DE            EC=2.5.1.56 {ECO:0000313|EMBL:EGV51075.1};
GN   Name=spsE {ECO:0000313|EMBL:EGV51075.1};
GN   ORFNames=Rifp1Sym_bw00100 {ECO:0000313|EMBL:EGV51075.1};
OS   endosymbiont of Riftia pachyptila (vent Ph05).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1048808 {ECO:0000313|EMBL:EGV51075.1, ECO:0000313|Proteomes:UP000004491};
RN   [1] {ECO:0000313|EMBL:EGV51075.1, ECO:0000313|Proteomes:UP000004491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
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:EGV51075.1}.
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DR   EMBL; AFOC01000050; EGV51075.1; -; Genomic_DNA.
DR   RefSeq; WP_005962874.1; NZ_AFOC01000050.1.
DR   AlphaFoldDB; G2DE65; -.
DR   Proteomes; UP000004491; Unassembled WGS sequence.
DR   GO; GO:0050462; F:N-acetylneuraminate synthase activity; IEA:UniProtKB-EC.
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;
KW   Transferase {ECO:0000313|EMBL:EGV51075.1}.
FT   DOMAIN          294..352
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50844"
SQ   SEQUENCE   355 AA;  40043 MW;  BB669ACB7D42604F CRC64;
     MTEIQIGGRV IGRHQPPFII AETGINHCGD LERAFKMIRA ARQVGADAVK FQTFQAEEFC
     SDPQQTYSYR SQGREVTESM LEMFRRHQFE PEQWRQICDC CDEEGIIFLS TPQNRSDLDL
     LLELEIPAIK VGSDDFTNLP QLRDYASTGL PMIVSAGMAD LDEVEQALRA IGTFKGHPTV
     LLHCVSQYPA PPEDANLRKL TSLRREYPEL ILGYSDHTQG VLGAVLAVAF GARVFEKHFT
     LDHDLPGPDH WFSADIGELQ QWVEAVRQAH RMLGSEAVEP TAVERKHRDA FRRSVVAIRN
     ISKNEPFSPE NLGVRRPGSG LKPNHMDAFF GHRATRTIAA GELIHWSDRE GNWVD
//
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