ID C5ZYJ3_9HELI Unreviewed; 370 AA.
AC C5ZYJ3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=General glycosylation pathway protein {ECO:0000313|EMBL:EES90211.1};
GN Name=pglE {ECO:0000313|EMBL:EES90211.1};
GN ORFNames=HCAN_1506 {ECO:0000313|EMBL:EES90211.1};
OS Helicobacter canadensis MIT 98-5491.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537970 {ECO:0000313|EMBL:EES90211.1, ECO:0000313|Proteomes:UP000007032};
RN [1] {ECO:0000313|EMBL:EES90211.1, ECO:0000313|Proteomes:UP000007032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX PubMed=19542273; DOI=10.1128/JB.00729-09;
RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA Weinstock G.M., Wren B.W., Pallen M.J.;
RT "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL J. Bacteriol. 191:5566-5567(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CM000776; EES90211.1; -; Genomic_DNA.
DR RefSeq; WP_006656991.1; NZ_CM000776.2.
DR AlphaFoldDB; C5ZYJ3; -.
DR STRING; 537970.HCAN_1506; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_7; -.
DR OrthoDB; 9766188at2; -.
DR Proteomes; UP000007032; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007032}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 370 AA; 41438 MW; 31B84D8D9974E5E3 CRC64;
MSFRIFLSPP QMGKNEQKYV DEAFRSNYIA PLGEFVNSFE LAMQDYTKSP NALALSSGTA
ALHLALRVAG ITKGDLVLAS TFTFIGSIVP ILYQGATPIF IDSDSSWNLS PKLLREALES
LKTKPKALIL THLYGQCAKI SEIAEICKEY GVLLIEDAAE SLGAFYKGQH TGTFGEFGAL
SFNGNKIITT SGGGMLLGKD SSQMQKARYY STQARENLPY YEHLDYGYNY RLSNICAAIG
LGQLEEIEDK VAKRRKIFDW YQENLSSEFV EFMPEIPDSR GNRWLSTLIF KEKKVNVMDL
VQILASKDIE SRPLWKPMHL QPLFRDSLNF CDGTSQNLFN NGICLPSGGA LERREIDEVS
GYILDYLKSL
//
