ID A0A268TF18_9HELI Unreviewed; 373 AA.
AC A0A268TF18;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:PAF43299.1};
GN ORFNames=BKH45_01280 {ECO:0000313|EMBL:PAF43299.1};
OS Helicobacter sp. 11S03491-1.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1476196 {ECO:0000313|EMBL:PAF43299.1, ECO:0000313|Proteomes:UP000216568};
RN [1] {ECO:0000313|EMBL:PAF43299.1, ECO:0000313|Proteomes:UP000216568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11S03491-1 {ECO:0000313|EMBL:PAF43299.1,
RC ECO:0000313|Proteomes:UP000216568};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAF43299.1}.
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; MLAO01000002; PAF43299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268TF18; -.
DR OrthoDB; 5342089at2; -.
DR Proteomes; UP000216568; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000216568}.
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 179
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 373 AA; 42103 MW; 4B5BD096C5DBCED4 CRC64;
MNPYSTQLIE EDDKKAVLHA LSSPHLTQGA LIEEFETKLS EYLGIKYILV FNSATSALYA
TYKAIGLDAN HHALTSPISF VATANMILEC GSLPIFCDIK RDGNINENLI ESLITPQTKA
IVSVDYAGNS VEAQSIQSIC KKYNLAFVSD SSHAFGGEYH QQKIGTLADA TIFSLHAIKP
ITTAEGGILA TNNSAIYEQA KLIRSHGVIK KKLWNTDVIT SGFNFRMTDL QAALGISQLK
KIQRFLNIRE EIAQFYDKAF ISNPYFFTLH QNLLHKTTNH LYPIILAPEF WCSKEELFKN
LQQEGLGVQV HYKPIYEFSL YRQILGEIEL PNARDFYRAE ISIPCHQKMN LNTAKETVDK
ILRVFEKLKI CKE
//
