PSEC_HELPY
ID PSEC_HELPY Reviewed; 375 AA.
AC O25130;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase;
DE EC=2.6.1.92 {ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16421095};
DE AltName: Full=Pseudaminic acid biosynthesis protein C;
GN Name=pseC; OrderedLocusNames=HP_0366;
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.
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).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16286454; DOI=10.1074/jbc.m511021200;
RA Schoenhofen I.C., McNally D.J., Vinogradov E., Whitfield D., Young N.M.,
RA Dick S., Wakarchuk W.W., Brisson J.R., Logan S.M.;
RT "Functional characterization of dehydratase/aminotransferase pairs from
RT Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid
RT and bacillosamine biosynthetic pathways.";
RL J. Biol. Chem. 281:723-732(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, PYRIDOXAL PHOSPHATE-BINDING SITE
RP LYS-183, AND MUTAGENESIS OF HIS-180 AND LYS-183.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16421095; DOI=10.1074/jbc.m512987200;
RA Schoenhofen I.C., Lunin V.V., Julien J.P., Li Y., Ajamian E., Matte A.,
RA Cygler M., Brisson J.R., Aubry A., Logan S.M., Bhatia S., Wakarchuk W.W.,
RA Young N.M.;
RT "Structural and functional characterization of PseC, an aminotransferase
RT involved in the biosynthesis of pseudaminic acid, an essential flagellar
RT modification in Helicobacter pylori.";
RL J. Biol. Chem. 281:8907-8916(2006).
CC -!- FUNCTION: Catalyzes the second step in the biosynthesis of pseudaminic
CC acid, a sialic-acid-like sugar that is used to modify flagellin. Uses
CC UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate
CC producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc.
CC {ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16421095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-
CC altrosamine = L-glutamate + UDP-2-acetamido-2,6-dideoxy-beta-L-
CC arabino-hex-4-ulose; Xref=Rhea:RHEA:31767, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:60101, ChEBI:CHEBI:63389; EC=2.6.1.92;
CC Evidence={ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16421095};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose
CC {ECO:0000269|PubMed:16421095};
CC Note=kcat is 43 min(-1) with (2E,6E)-farnesyl UDP-2-acetamido-2,6-
CC dideoxy-beta-L-arabino-4-hexulose as substrate.;
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07433.1; -; Genomic_DNA.
DR PIR; F64565; F64565.
DR RefSeq; NP_207164.1; NC_000915.1.
DR RefSeq; WP_000657303.1; NC_018939.1.
DR PDB; 2FN6; X-ray; 2.48 A; A/B=1-375.
DR PDB; 2FNI; X-ray; 3.00 A; A/B=1-375.
DR PDB; 2FNU; X-ray; 1.50 A; A/B=1-375.
DR PDBsum; 2FN6; -.
DR PDBsum; 2FNI; -.
DR PDBsum; 2FNU; -.
DR AlphaFoldDB; O25130; -.
DR SMR; O25130; -.
DR STRING; 85962.C694_01855; -.
DR PaxDb; O25130; -.
DR EnsemblBacteria; AAD07433; AAD07433; HP_0366.
DR KEGG; hpy:HP_0366; -.
DR PATRIC; fig|85962.47.peg.388; -.
DR eggNOG; COG0399; Bacteria.
DR OMA; QVHYKPI; -.
DR PhylomeDB; O25130; -.
DR BioCyc; MetaCyc:HP0366-MON; -.
DR BRENDA; 2.6.1.92; 2604.
DR EvolutionaryTrace; O25130; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IBA:GO_Central.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03588; PseC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..375
FT /note="UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine
FT transaminase"
FT /id="PRO_0000418957"
FT BINDING 6
FT /ligand="substrate"
FT BINDING 26..29
FT /ligand="substrate"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 178
FT /ligand="substrate"
FT BINDING 228
FT /ligand="substrate"
FT BINDING 313..316
FT /ligand="substrate"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 180
FT /note="H->N: Impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:16421095"
FT MUTAGEN 183
FT /note="K->R: Strongly impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:16421095"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 246..264
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:2FNU"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2FNU"
FT HELIX 355..372
FT /evidence="ECO:0007829|PDB:2FNU"
SQ SEQUENCE 375 AA; 42399 MW; CE6AAD3D475FDF64 CRC64;
MKEFAYSEPC LDKEDKKAVL EVLNSKQLTQ GKRSLLFEEA LCEFLGVKHA LVFNSATSAL
LTLYRNFSEF SADRNEIITT PISFVATANM LLESGYTPVF AGIKNDGNID ELALEKLINE
RTKAIVSVDY AGKSVEVESV QKLCKKHSLS FLSDSSHALG SEYQNKKVGG FALASVFSFH
AIKPITTAEG GAVVTNDSEL HEKMKLFRSH GMLKKDFFEG EVKSIGHNFR LNEIQSALGL
SQLKKAPFLM QKREEAALTY DRIFKDNPYF TPLHPLLKDK SSNHLYPILM HQKFFTCKKL
ILESLHKRGI LAQVHYKPIY QYQLYQQLFN TAPLKSAEDF YHAEISLPCH ANLNLESVQN
IAHSVLKTFE SFKIE
