ID Q1K172_DESA6 Unreviewed; 357 AA.
AC Q1K172;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=N-acylneuraminate-9-phosphate synthase {ECO:0000313|EMBL:EAT16136.1};
DE EC=2.5.1.57 {ECO:0000313|EMBL:EAT16136.1};
GN ORFNames=Dace_1600 {ECO:0000313|EMBL:EAT16136.1};
OS Desulfuromonas acetoxidans (strain DSM 684 / 11070).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Desulfuromonas.
OX NCBI_TaxID=281689 {ECO:0000313|EMBL:EAT16136.1, ECO:0000313|Proteomes:UP000005695};
RN [1] {ECO:0000313|EMBL:EAT16136.1, ECO:0000313|Proteomes:UP000005695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070 {ECO:0000313|Proteomes:UP000005695};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Desulfuromonas acetoxidans DSM
RT 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT16136.1, ECO:0000313|Proteomes:UP000005695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070 {ECO:0000313|Proteomes:UP000005695};
RG US DOE Joint Genome Institute (JGI-PGF);
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., Bruce D.,
RA Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Desulfuromonas acetoxidans
RT DSM 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:EAT16136.1}.
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DR EMBL; AAEW02000006; EAT16136.1; -; Genomic_DNA.
DR RefSeq; WP_005999282.1; NZ_AAEW02000006.1.
DR AlphaFoldDB; Q1K172; -.
DR OrthoDB; 9781701at2; -.
DR Proteomes; UP000005695; Unassembled WGS sequence.
DR GO; GO:0047444; F:N-acylneuraminate-9-phosphate 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; IPR020007; N-AcNeuraminate_synthase.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR NCBIfam; TIGR03569; NeuB_NnaB; 1.
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 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:UP000005695};
KW Transferase {ECO:0000313|EMBL:EAT16136.1}.
FT DOMAIN 307..357
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 357 AA; 39481 MW; EC696B3874B1B903 CRC64;
MHTYIIAEVG VNHNGSVELA KKLIHVAKDC GADAVKFQTF KTERLVTSSA KKAVYQDEND
NSTTTQAEML GRLELTIDDF VELDRECRAA GVDFLTTCFD SESLLTIMDE LHLSVLKIGS
GDLTNLPFLI EHAKTGAKLV VSTGMATLSE VEDAMAALAF GYLEEEKEMP ESYQWLKRHY
FSSEKIEQLS DRVTLLHCVT DYPAQYRDLN LDAIGQLRQA YKLNVGYSDH SLGIEACCAA
VALGAVCIEK HLTLDKGLSG PDHAASASPE EFRLLVNAIR NLELALQPRI KSPTKRELAN
LEVARKYLVA KQDIEQGEVF SVENVEIKRS AFGMSPSQYW NVLGHKAIKS YSAGDSL
//
