ID D3UJE3_HELM1 Unreviewed; 382 AA.
AC D3UJE3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Putative aminotransferase DegT/DnrJ/EryC1/StrS family {ECO:0000313|EMBL:CBG40619.1};
GN OrderedLocusNames=HMU13660 {ECO:0000313|EMBL:CBG40619.1};
OS Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
OS (Campylobacter mustelae).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40619.1, ECO:0000313|Proteomes:UP000001522};
RN [1] {ECO:0000313|EMBL:CBG40619.1, ECO:0000313|Proteomes:UP000001522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC {ECO:0000313|Proteomes:UP000001522};
RX PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA Bentley S.D.;
RT "Comparative genomics and proteomics of Helicobacter mustelae, an
RT ulcerogenic and carcinogenic gastric pathogen.";
RL BMC Genomics 11:164-164(2010).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; FN555004; CBG40619.1; -; Genomic_DNA.
DR RefSeq; WP_013023685.1; NC_013949.1.
DR AlphaFoldDB; D3UJE3; -.
DR STRING; 679897.HMU13660; -.
DR KEGG; hms:HMU13660; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_7; -.
DR Proteomes; UP000001522; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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 Aminotransferase {ECO:0000313|EMBL:CBG40619.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000001522};
KW Transferase {ECO:0000313|EMBL:CBG40619.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 382 AA; 42569 MW; F905DF98B7341DB6 CRC64;
MQIPFLDLTS LNKPYFSPFL RRTKEIFAQS DFINGAACKQ FEQEFARYIG ARYCLGVGNG
TDALEIAIKA LNLPKGSQII LPANTFKASC EAILNTGHKA VIVDCNEDYT INIPSLKRAL
TPGSAAILVV HLYGRICDMA SILEIARSYE LALIEDCSQA HGARIKIGNK MLFAGNIGDI
ATFSFYPSKN LGAIGDGGCI LSNDKNLISR CQNIANHCPN PQEKIHFIGR NSRLDSLQAA
FLSLKLPDLE AQNQHRQKIA KLYREKLCNI HALVLPQIPV FAHQCVWHLY VVRLQGELEG
KREDLMEFLR ERGIETRVHY AQNLTKLKEI HSNISTITSP TPNANNWEAN LLSLPMGTHL
QEKDIIIIAE SIQAFCKLIT KA
//
