ID A0A1E3L0I6_9BACL Unreviewed; 359 AA.
AC A0A1E3L0I6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=N-acetylneuraminate synthase {ECO:0000313|EMBL:ODP27307.1};
DE EC=2.5.1.56 {ECO:0000313|EMBL:ODP27307.1};
GN Name=neuB {ECO:0000313|EMBL:ODP27307.1};
GN ORFNames=PTI45_03241 {ECO:0000313|EMBL:ODP27307.1};
OS Paenibacillus nuruki.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP27307.1, ECO:0000313|Proteomes:UP000094578};
RN [1] {ECO:0000313|EMBL:ODP27307.1, ECO:0000313|Proteomes:UP000094578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP27307.1,
RC ECO:0000313|Proteomes:UP000094578};
RA Kim S.-J.;
RT "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT traditional nuruk.";
RL Submitted (AUG-2016) 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:ODP27307.1}.
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DR EMBL; MDER01000060; ODP27307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3L0I6; -.
DR STRING; 1886670.PTI45_03241; -.
DR PATRIC; fig|1886670.3.peg.3295; -.
DR Proteomes; UP000094578; 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; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR PANTHER; PTHR42966; N-ACETYLNEURAMINATE SYNTHASE; 1.
DR PANTHER; PTHR42966:SF2; PSEUDAMINIC ACID SYNTHASE; 1.
DR Pfam; PF03102; NeuB; 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:UP000094578};
KW Transferase {ECO:0000313|EMBL:ODP27307.1}.
FT DOMAIN 300..359
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 359 AA; 40663 MW; BDADAA6F66036471 CRC64;
MKYDSSIKIN EKEISINSPT YFIADIAANH DGDLERAKEL IWLAKEAGAD AAKFQHFKAE
KIVSDYGFKE LNGLSSHQSN WKNSVFDTYK KYEFDRDWNQ ELIATAQSAQ IDFMTTPYDY
AAITSVDAHV PAYKVGSGDI SWVDFIEEIA KKEKPIILAT GASEISDVER AVQTILKYNR
QLILLQCNTN YTGNLENLGY VNLRVLQTYA IKYPHMILGL SDHTPGHATV LGAITLGARV
IEKHFTDDNN RVGPDHLFSM NPTTWRDMID RSRELEAALG DGTKRVEDNE KDAFIVQRRC
LRLTKSLKAG DIIKDEDVEA LRPAPKDSIH PYEKDIVVGQ ILLIDKNQGD ALYMKDMRR
//
