ID A4G468_HERAR Unreviewed; 351 AA.
AC A4G468;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=N-acylneuraminate-9-phosphate synthase {ECO:0000313|EMBL:CAL61305.1};
DE EC=2.5.1.57 {ECO:0000313|EMBL:CAL61305.1};
GN OrderedLocusNames=HEAR1126 {ECO:0000313|EMBL:CAL61305.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL61305.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL61305.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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DR EMBL; CU207211; CAL61305.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G468; -.
DR STRING; 204773.HEAR1126; -.
DR KEGG; har:HEAR1126; -.
DR eggNOG; COG2089; Bacteria.
DR HOGENOM; CLU_040465_0_1_4; -.
DR OrthoDB; 9781701at2; -.
DR Proteomes; UP000006697; Chromosome.
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; 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:UP000006697};
KW Transferase {ECO:0000313|EMBL:CAL61305.1}.
FT DOMAIN 295..351
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 351 AA; 38270 MW; 76C59ECCA575E0B1 CRC64;
MAQELVIAGR LIGRGHAPFV IAEMSGNHNQ SLERALQIVD AAARSGAHAL KIQTYTPDTM
TIDLDEREFH IGDPNSLWSG TSLYKLYGEA YTPWEWHEAI FARAREHGMI PFSSPFDASA
VDFLESLNVA CYKIASFENT DLPLIRRVAA TGKPLIISTG MATAAELDES VRAARQAGCK
DLILLKCTST YPATAANTNI LTIPHMRELF GCEIGLSDHT MGIGVSVASV ALGAVVIEKH
FTLDRADGGV DSTFSMEPAE MAQLVLETGR AWEALGRVSY GPTEVEKKSL QYRRSLYVVQ
DIKAGDVLTQ ENVRAIRPGL GLPTKYLEQL LGKTVKSDVK RGTALTWEMI G
//
