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Database: UniProt
Entry: D1PNQ3_9FIRM
LinkDB: D1PNQ3_9FIRM
Original site: D1PNQ3_9FIRM 
ID   D1PNQ3_9FIRM            Unreviewed;       331 AA.
AC   D1PNQ3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=N-acetylneuraminate synthase {ECO:0000313|EMBL:EFB76188.1};
DE            EC=2.5.1.56 {ECO:0000313|EMBL:EFB76188.1};
GN   Name=neuB {ECO:0000313|EMBL:EFB76188.1};
GN   ORFNames=SUBVAR_05974 {ECO:0000313|EMBL:EFB76188.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB76188.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB76188.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB76188.1,
RC   ECO:0000313|Proteomes:UP000003438};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2009) 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:EFB76188.1}.
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DR   EMBL; ACBY02000023; EFB76188.1; -; Genomic_DNA.
DR   RefSeq; WP_007047348.1; NZ_GG704769.1.
DR   AlphaFoldDB; D1PNQ3; -.
DR   STRING; 411471.SUBVAR_05974; -.
DR   GeneID; 78306139; -.
DR   eggNOG; COG2089; Bacteria.
DR   HOGENOM; CLU_040465_0_0_9; -.
DR   OrthoDB; 9814210at2; -.
DR   Proteomes; UP000003438; 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; 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   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:UP000003438};
KW   Transferase {ECO:0000313|EMBL:EFB76188.1}.
FT   DOMAIN          279..331
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50844"
SQ   SEQUENCE   331 AA;  35982 MW;  556CA9C6ED05FEE3 CRC64;
     MPVTIIAEAG VNHNGDLEMA KRMALAAKEC GADIVKYQTA VPELVVSKFA EKAAYQKETT
     DAAESQLDMI RKLHFSFDGH RELKEYCDSI GIQYLSAPFD IPSVRFLGTL NLPLIKIPSG
     EITNLPYLEE VAKLHTPVLL STGMSNLNEI TDALGILDDG GCPEATVLHC NTQYPTPYED
     ANLTAMLELF DQFGLPVGLS DHTPGWECDV AAAVLGATVI EKHFTLDKTL PGPDQQASLD
     PTEFKAMVQA VRHVEAALGD GHKHLTASEA PNKAVARKSI VAARPIKAGE VFTADNLTTK
     RPGDGISPMR WYDVLGKTAP RDFDEDEKIQ L
//
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