PSEFG_HELPY
ID PSEFG_HELPY Reviewed; 517 AA.
AC O25093;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Pseudaminic acid cytidylyltransferase and UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase;
DE Includes:
DE RecName: Full=Pseudaminic acid cytidylyltransferase;
DE EC=2.7.7.81;
DE AltName: Full=Pseudaminic acid biosynthesis protein F;
DE Short=PseF;
DE AltName: Full=Pseudaminic acid cytidylyltransferase HP_0326A;
DE Includes:
DE RecName: Full=UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase;
DE EC=3.6.1.57;
DE AltName: Full=Pseudaminic acid biosynthesis protein G;
DE Short=PseG;
DE AltName: Full=UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase HP_0326B;
GN OrderedLocusNames=HP_0326;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP PATHWAY, FUNCTION, AND COFACTOR.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16751642; DOI=10.1093/glycob/cwl010;
RA Schoenhofen I.C., McNally D.J., Brisson J.R., Logan S.M.;
RT "Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori:
RT synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction.";
RL Glycobiology 16:8C-14C(2006).
CC -!- FUNCTION: Catalyzes the fourth and sixth steps in the biosynthesis of
CC pseudaminic acid, a sialic-acid-like sugar that is used to modify
CC flagellin. The C-terminus mediates the fourth step of the pathway and
CC catalyzes the removal of UDP from C-1 of UDP-2,4-diacetamido-2,4,6-
CC trideoxy-beta-L-altropyranose forming 2,4-diacetamido-2,4,6-trideoxy-
CC beta-L-altropyranose. The N-terminal part mediates the last step of the
CC pathway by mediating activation of pseudaminic acid with CMP by forming
CC CMP-pseudaminic acid. {ECO:0000269|PubMed:16751642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose = 2,4-
CC diacetamido-2,4,6-trideoxy-beta-L-altrose + H(+) + UDP;
CC Xref=Rhea:RHEA:31803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:63283, ChEBI:CHEBI:63417; EC=3.6.1.57;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + pseudaminate = CMP-pseudaminate + diphosphate;
CC Xref=Rhea:RHEA:32083, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:63282, ChEBI:CHEBI:63680; EC=2.7.7.81;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16751642};
CC Note=Mg(2+) is required for pseudaminic acid cytidylyltransferase
CC activity. {ECO:0000269|PubMed:16751642};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- MISCELLANEOUS: In publications, PseF (HP_0326A) and PseG (HP_0326B) are
CC separated into 2 separate ORFs (PubMed:16751642). However, these 2
CC enzymes are fused into a single protein in strain ATCC 700392 / 26695.
CC {ECO:0000305|PubMed:16751642}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CMP-NeuNAc
CC synthase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PseG family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD07393.1; -; Genomic_DNA.
DR PIR; F64560; F64560.
DR RefSeq; NP_207124.1; NC_000915.1.
DR RefSeq; WP_001201399.1; NC_018939.1.
DR AlphaFoldDB; O25093; -.
DR SMR; O25093; -.
DR DIP; DIP-3686N; -.
DR IntAct; O25093; 1.
DR MINT; O25093; -.
DR STRING; 85962.C694_01650; -.
DR PaxDb; O25093; -.
DR EnsemblBacteria; AAD07393; AAD07393; HP_0326.
DR KEGG; hpy:HP_0326; -.
DR PATRIC; fig|85962.8.peg.340; -.
DR eggNOG; COG3980; Bacteria.
DR BioCyc; MetaCyc:HP0326-MON; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IBA:GO_Central.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR020039; PseF.
DR Pfam; PF02348; CTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR03584; PseF; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..517
FT /note="Pseudaminic acid cytidylyltransferase and UDP-2,4-
FT diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase"
FT /id="PRO_0000418936"
FT REGION 1..208
FT /note="Pseudaminic acid cytidylyltransferase"
FT REGION 209..517
FT /note="UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-
FT altropyranose hydrolase"
FT ACT_SITE 244
FT /note="Proton acceptor; for UDP-2,4-diacetamido-2,4,6-
FT trideoxy-beta-L-altropyranose hydrolase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 517 AA; 58934 MW; DF78B98ED41F6DA2 CRC64;
MRAIAIVLAR SSSKRIKNKN IIDFFNKPML AYPIEVALNS KLFEKVFISS DSMEYVNLAK
NYGASFLNLR PKILADDRAT TLEVMAYHME ELELKDEDIA CCLYGASALL QEKHLKNAFE
TLNKNQNTDY VFTCSPFSAS PYRSFSLENG VQMAFKEHSN TRTQDLKTLY HDAGLLYMGK
AQAFKEMRPI FSQNSIALEL SPLEVQDIAH FRRFRISQAQ IQPFEKRMPV KILCDCFLTS
GLGHVRRCEK ILSFIEKLGV EASLYLHKQN NISAFLEGVG GNDFLITDSY CLNSKDFYLL
KEKAKSLMVI EDTEHAKGFY PKNTKILNFT LNALKHYHHL SKDYQYYLGV GFYPVDARFI
YDRPINTENK EVLITLGGSE QKTLKEIVKI LENKNVNLHI ISPYTPKNPP KNTHYYSPLN
PLEFSSLMKS CACAISAAGQ TLYELALSQT PSLILPIASN QIIQSKEFES LGIFKQTSLK
TLAKDFENLQ IQKNQAWAKN LVFGDKLEGA LREFLEI
