ID   PSEC_CAMJJ              Reviewed;         376 AA.
AC   Q5QKR7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase;
DE            EC=2.6.1.92 {ECO:0000250|UniProtKB:Q0P8W3};
DE   AltName: Full=Pseudaminic acid biosynthesis protein C;
GN   Name=pseC; OrderedLocusNames=CJJ81176_1311;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=81-176;
RX   PubMed=11461915; DOI=10.1074/jbc.m104529200;
RA   Thibault P., Logan S.M., Kelly J.F., Brisson J.-R., Ewing C.P., Trust T.J.,
RA   Guerry P.;
RT   "Identification of the carbohydrate moieties and glycosylation motifs in
RT   Campylobacter jejuni flagellin.";
RL   J. Biol. Chem. 276:34862-34870(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=81-176;
RX   PubMed=16861657; DOI=10.1128/iai.00210-06;
RA   Hofreuter D., Tsai J., Watson R.O., Novik V., Altman B., Benitez M.,
RA   Clark C., Perbost C., Jarvie T., Du L., Galan J.E.;
RT   "Unique features of a highly pathogenic Campylobacter jejuni strain.";
RL   Infect. Immun. 74:4694-4707(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RC   STRAIN=81-176;
RX   PubMed=16684771; DOI=10.1074/jbc.m603777200;
RA   McNally D.J., Hui J.P., Aubry A.J., Mui K.K., Guerry P., Brisson J.R.,
RA   Logan S.M., Soo E.C.;
RT   "Functional characterization of the flagellar glycosylation locus in
RT   Campylobacter jejuni 81-176 using a focused metabolomics approach.";
RL   J. Biol. Chem. 281:18489-18498(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:16684771}.
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:0000250|UniProtKB:Q0P8W3};
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR   EMBL; AY102622; AAP12669.1; -; Genomic_DNA.
DR   EMBL; DQ493920; ABF83717.1; -; Genomic_DNA.
DR   EMBL; CP000538; EAQ72854.1; -; Genomic_DNA.
DR   RefSeq; WP_002869094.1; NC_008787.1.
DR   AlphaFoldDB; Q5QKR7; -.
DR   SMR; Q5QKR7; -.
DR   STRING; 354242.CJJ81176_1311; -.
DR   EnsemblBacteria; EAQ72854; EAQ72854; CJJ81176_1311.
DR   KEGG; cjj:CJJ81176_1311; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_0_3_7; -.
DR   OMA; QVHYKPI; -.
DR   Proteomes; UP000000646; 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   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..376
FT                   /note="UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine
FT                   transaminase"
FT                   /id="PRO_0000418959"
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;  42317 MW;  2E603ACCFEC87BE2 CRC64;
     MITYSHQNID QSDIDALTKA LKDEILTGGK KVDEFEEALC EYIGVKHACV LNSATSALHL
     AYTALGIKEK IVLTTPLTFA ATANAALIAG AKVEFIDIKN DGNIDEKKLE ARLVKNSTDI
     GAISVVDFGG NSVEMDEISN LAKKYNIPLI DDASHALGSE YKGKKVGSMA DLSIFSFHPV
     KPITTFEGGA VVSNNKELIS KIKLLRSHGI VKKRLWDSDM IELGYNYRLS DVACALGINQ
     LKKLDHNLEK REEITSFYDK EFEKNHYFST IKIKDYKKSS RHLYPILLFP EFYCQKEELF
     ESLLHAGIGV QVHYKPTYEF SFYKKLLGEI RLQNADNFYK AELSIPCHQE MNLKDAKFVK
     DTLFSILEKV KKGYCG