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Database: UniProt
Entry: Q12JI6_SHEDO
LinkDB: Q12JI6_SHEDO
Original site: Q12JI6_SHEDO 
ID   Q12JI6_SHEDO            Unreviewed;       359 AA.
AC   Q12JI6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=N-acetylneuraminate synthase {ECO:0000313|EMBL:ABE56390.1};
DE            EC=2.5.1.56 {ECO:0000313|EMBL:ABE56390.1};
GN   OrderedLocusNames=Sden_3113 {ECO:0000313|EMBL:ABE56390.1};
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE56390.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE56390.1, ECO:0000313|Proteomes:UP000001982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC   {ECO:0000313|Proteomes:UP000001982};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000302; ABE56390.1; -; Genomic_DNA.
DR   RefSeq; WP_011497536.1; NC_007954.1.
DR   AlphaFoldDB; Q12JI6; -.
DR   STRING; 318161.Sden_3113; -.
DR   KEGG; sdn:Sden_3113; -.
DR   eggNOG; COG2089; Bacteria.
DR   HOGENOM; CLU_040465_0_1_6; -.
DR   OrthoDB; 9781701at2; -.
DR   Proteomes; UP000001982; Chromosome.
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; IPR020030; Pseudaminic_synth_PseI.
DR   InterPro; IPR013974; SAF.
DR   NCBIfam; TIGR03586; PseI; 1.
DR   PANTHER; PTHR42966; N-ACETYLNEURAMINATE SYNTHASE; 1.
DR   PANTHER; PTHR42966:SF2; PSEUDAMINIC 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   Reference proteome {ECO:0000313|Proteomes:UP000001982};
KW   Transferase {ECO:0000313|EMBL:ABE56390.1}.
FT   DOMAIN          294..352
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50844"
SQ   SEQUENCE   359 AA;  39048 MW;  EBA533CC6262BCDD CRC64;
     MFKASITIDG RHIGPEYQPY IIAELSGNHK GSLSQALAMI DAAAASGVDA IKIQTYTANT
     ITLQHDGPEF RINGGLWKGR TLFDLYEEAH TPWEWHKSLF EHAKKQNVTL FSSPFDLKAI
     ELLESCECPA YKISSFEIND IGLIMAAAKT GKPIVMSTGL ATLAEIEEAV EAVANAGGTQ
     LALLHCISGY PTPIEDCNLK TVADLCQRFN FPIGLSDHTT DILASVTSVA LGASIIEKHF
     TLDKTDGGVD AAFSLEPDEF GLLKKETQRA HSALGYAGYD IKPSEAGGRD FRRSVYVADD
     IRKGELFTAS NVRSVRPGLG LHTRYLPQII GQKSSQDIAF GSPMKEEYLS VPLLKRDPS
//
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