PSEC_CAMJE
ID PSEC_CAMJE Reviewed; 376 AA.
AC Q0P8W3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
DE AltName: Full=Pseudaminic acid biosynthesis protein C;
GN Name=pseC; OrderedLocusNames=Cj1294;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700819 / NCTC 11168;
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 [3]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16690622; DOI=10.1074/jbc.m511714200;
RA Vijayakumar S., Merkx-Jacques A., Ratnayake D.B., Gryski I., Obhi R.K.,
RA Houle S., Dozois C.M., Creuzenet C.;
RT "Cj1121c, a novel UDP-4-keto-6-deoxy-GlcNAc C-4 aminotransferase essential
RT for protein glycosylation and virulence in Campylobacter jejuni.";
RL J. Biol. Chem. 281:27733-27743(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}.
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};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.052 mM for UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine
CC {ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16690622};
CC KM=1.28 mM for UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine
CC {ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16690622};
CC Note=kcat is 4 min(-1) (PubMed:16286454). kcat is 11.5 min(-1)
CC (PubMed:16690622). {ECO:0000269|PubMed:16286454,
CC ECO:0000269|PubMed:16690622};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35408.1; -; Genomic_DNA.
DR PIR; C81272; C81272.
DR RefSeq; WP_002856503.1; NC_002163.1.
DR RefSeq; YP_002344684.1; NC_002163.1.
DR AlphaFoldDB; Q0P8W3; -.
DR SMR; Q0P8W3; -.
DR IntAct; Q0P8W3; 19.
DR STRING; 192222.Cj1294; -.
DR PaxDb; Q0P8W3; -.
DR PRIDE; Q0P8W3; -.
DR EnsemblBacteria; CAL35408; CAL35408; Cj1294.
DR GeneID; 905586; -.
DR KEGG; cje:Cj1294; -.
DR PATRIC; fig|192222.6.peg.1276; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_7; -.
DR OMA; QVHYKPI; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..376
FT /note="UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine
FT transaminase"
FT /id="PRO_0000418958"
FT BINDING 4
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 24..27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311..314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 42450 MW; 1E0997AC5EAD758C CRC64;
MLTYSHQNID QSDIDTLTKA LKDEILTGGK KVNEFEEALC EYMGVKHACV LNSATSALHL
AYTALGVQEK IVLTTPLTFA ATANAALMAG AKVEFIDIKN DGNIDEKKLE ARLLKESENI
GAISVVDFAG NSVEMDEISN LTKKYNIPLI DDASHALGAL YKSEKVGKKA DLSIFSFHPV
KPITTFEGGA VVSDNEELID KIKLLRSHGI VKKRLWDSDM VELGYNYRLS DVACALGINQ
LKKLDHNLEK REEIANFYDK EFEKNPYFST IKIKDYKKSS RHLYPILLFP EFYCQKEELF
ESLLHAGIGV QVHYKPTYEF SFYKKLLGEI KLQNADNFYK AELSIPCHQE MNLKDAKFVK
DTLFSILEKV KKGYCG
