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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//