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Database: UniProt
Entry: Q12PQ1_SHEDO
LinkDB: Q12PQ1_SHEDO
Original site: Q12PQ1_SHEDO 
ID   Q12PQ1_SHEDO            Unreviewed;       350 AA.
AC   Q12PQ1;
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:ABE54575.1};
DE            EC=2.5.1.56 {ECO:0000313|EMBL:ABE54575.1};
GN   OrderedLocusNames=Sden_1289 {ECO:0000313|EMBL:ABE54575.1};
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:ABE54575.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE54575.1, 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; ABE54575.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12PQ1; -.
DR   STRING; 318161.Sden_1289; -.
DR   KEGG; sdn:Sden_1289; -.
DR   eggNOG; COG2089; Bacteria.
DR   HOGENOM; CLU_040465_0_1_6; -.
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:ABE54575.1}.
FT   DOMAIN          292..350
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50844"
SQ   SEQUENCE   350 AA;  38277 MW;  473C4A2D6C06DA5A CRC64;
     MININGRHIG DAQPTYIIAE LSANHGGSLE QAKIMIQKAK QAGADAVKIQ TYRADTITLN
     CDKADFRLPS GNAWEAHNTL YALYQEAYTP WEWNKALFEE ARRIGITLFS SPFDETAVDL
     LESLNAPAYK IASPEITDIG LLKYVARTGK PIILSTGIAD LADIELAVET LRANGCEALA
     ILKCTTAYPT PYSECNLRTI ADIGKRFSCV AGLSDHTLGL ASPIAATALG GKIIEKHFIL
     DKTDNSVDAF FSLDEHEFSQ MVTEVRNAEL ALGTISYEIS GSANKNKLAR RSLYYSQAIK
     AGEVITNENV KSVRPGFGLH PKHFDAILGL RLKHDVEFGD RVSLLDVDTE
//
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