ID Q6EB20_CAMJU Unreviewed; 361 AA.
AC Q6EB20;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Tgh42 {ECO:0000313|EMBL:AAS99065.1};
OS Campylobacter jejuni.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197 {ECO:0000313|EMBL:AAS99065.1};
RN [1] {ECO:0000313|EMBL:AAS99065.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TGH 9011 {ECO:0000313|EMBL:AAS99065.1};
RX PubMed=15231810; DOI=10.1128/JB.186.14.4781-4795.2004;
RA Poly F., Threadgill D., Stintzi A.;
RT "Identification of Campylobacter jejuni ATCC 43431-specific genes by whole
RT microbial genome comparisons.";
RL J. Bacteriol. 186:4781-4795(2004).
RN [2] {ECO:0000313|EMBL:AAW79070.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RM1047 {ECO:0000313|EMBL:AAW79070.1};
RX PubMed=15956396; DOI=10.1128/JCM.43.6.2771-2781.2005;
RA Parker C.T., Horn S.T., Gilbert M., Miller W.G., Woodward D.L.,
RA Mandrell R.E.;
RT "Comparison of Campylobacter jejuni lipooligosaccharide biosynthesis loci
RT from a variety of sources.";
RL J. Clin. Microbiol. 43:2771-2781(2005).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; AY501976; AAS99065.1; -; Genomic_DNA.
DR EMBL; AY800272; AAW79070.1; -; Genomic_DNA.
DR RefSeq; WP_002876187.1; NZ_SYUD01000001.1.
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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 361 AA; 41593 MW; D1C3197BFA630859 CRC64;
MIKFLDLKQI NDRFNTEFIT KFKEILESGW YILGKQCEKF ENNFAKYCGV KHCIGVANGL
DALRLIIKAY NFKENDEIIV PANTYIASIL AITDNKCKPI LIEPDINTYN INPDLIEEKI
TKKTKAIMVV HLYGQVCDME KIQLLANKYN LKIIEDCAQA HGAIYKDKRV GNLGDAAGFS
FYPGKNLGAL GDAGCICTND DNFASKIRAL ANYGSHKKYE NLYIGLNSRL DEIQAAFLDI
KLKYLDEDNN KRKNIANFYL QNIKNENIIL PSNKFDHVWH LFIVKTKLRD ELQHYLNNHD
IQTIIHYPIP PHKQKCYKDL NHLQLPVTEN IHQEVLSLPI SPTMKENDFK KVADILNKWK
V
//
