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
//