ID I0ET77_HELCM Unreviewed; 375 AA.
AC I0ET77;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN OrderedLocusNames=HCD_05720 {ECO:0000313|EMBL:AFI06146.1};
OS Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163745 {ECO:0000313|EMBL:AFI06146.1, ECO:0000313|Proteomes:UP000005013};
RN [1] {ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 99-5656.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFI06146.1, ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RX PubMed=24358262;
RA Kersulyte D., Rossi M., Berg D.E.;
RT "Sequence Divergence and Conservation in Genomes ofHelicobacter cetorum
RT Strains from a Dolphin and a Whale.";
RL PLoS ONE 8:E83177-E83177(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP003481; AFI06146.1; -; Genomic_DNA.
DR RefSeq; WP_014659634.1; NC_017735.1.
DR AlphaFoldDB; I0ET77; -.
DR STRING; 1163745.HCD_05720; -.
DR KEGG; hcm:HCD_05720; -.
DR PATRIC; fig|1163745.3.peg.1210; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_7; -.
DR OrthoDB; 9804474at2; -.
DR Proteomes; UP000005013; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..340
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 375 AA; 43157 MW; 8F680BA775EAD0E3 CRC64;
MTFEPYPFER LRALFKDITP LKKGLDLGIG EPRFETPKFI QDTLKEHANS LNIYPKSAFE
ESLRVAQRSF FKRRFNIELK ENELVSTLGS REVLFNFPSF VLFNHKNPTI AYPNPFYQIY
EGASKFVKAK SILMPLTKEN NFTPSLNEKE LEEVNLVILN SPNNPTGRTL SLEELVAWVK
LALKYNFILI NDECYSEIYE DSPPPSLLEA SILADNKEFK NVLVVHSLSK RSSVPGLRSG
FIAGDSHILE NYKAFRTYLG YTSANAIQKA SEAAWLDEEH AKFFRNIYAN NLKLARKIFK
DTLIYPNSFY VYLPVKNGES FAKMLYQNEG ITTLPALYLG RNHIGTDYVR LALVYDTPLL
EKPLEMIETY RENHA
//
