ID E6NSK9_HELPQ Unreviewed; 375 AA.
AC E6NSK9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Spore coat polysaccharide biosynthesis protein C {ECO:0000313|EMBL:BAJ60125.1};
GN OrderedLocusNames=HPF57_1051 {ECO:0000313|EMBL:BAJ60125.1};
OS Helicobacter pylori (strain F57).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ60125.1, ECO:0000313|Proteomes:UP000008082};
RN [1] {ECO:0000313|EMBL:BAJ60125.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ60125.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Evolution in an oncogenic bacterial species with extreme genome
RT plasticity: Helicobacter pylori East Asian genomes.";
RL BMC Microbiol. 11:104-104(2011).
RN [2] {ECO:0000313|EMBL:BAJ60125.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ60125.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Birth and death of genes linked to chromosomal inversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011945; BAJ60125.1; -; Genomic_DNA.
DR RefSeq; WP_000657240.1; NC_017367.1.
DR AlphaFoldDB; E6NSK9; -.
DR KEGG; hex:HPF57_1051; -.
DR PATRIC; fig|866346.4.peg.1129; -.
DR HOGENOM; CLU_033332_0_3_7; -.
DR Proteomes; UP000008082; Chromosome.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 375 AA; 42634 MW; AE7048943B490BAE CRC64;
MKEFAYSEPC LDEEDKKAVL EVLNSKQLTQ GKRSLLFEEA LCEFLGVKHA LVFNSATSAL
LTLYRNFSDF NADCNEIITT PISFVATANM LLESGYKPVF AEIKNDGNID ELVLEKLINE
RTKAIVSVDY AGKSVEIESI QKLCKRHSLS FLSDSSHALG SEYQNKKVGG FALASVFSFH
AIKPITTAEG GAVVTNDGEL YEKMKWFRSH GMIKKDFFEG EVKSIGHNFR LNEIQSALGL
SQLKKAPLLM QKREEIALVY DRIFKDNPYF TPLHPLLKDK SSNHLYPILM RQKFFTCKKL
ILENLHKRGI LAQVHYKPIY QYQLYQQLFN TAPLKSAEDF YRAEISLPCH ANLDLESVQN
IAHGVLKTFE DLKVE
//
