ID Q0PAC8_CAMJE Unreviewed; 389 AA.
AC Q0PAC8;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:CAL34890.1};
DE EC=2.6.1.1 {ECO:0000313|EMBL:CAL34890.1};
GN Name=aspB {ECO:0000313|EMBL:CAL34890.1};
GN OrderedLocusNames=Cj0762c {ECO:0000313|EMBL:CAL34890.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34890.1, ECO:0000313|Proteomes:UP000000799};
RN [1] {ECO:0000313|EMBL:CAL34890.1, ECO:0000313|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; AL111168; CAL34890.1; -; Genomic_DNA.
DR PIR; B81347; B81347.
DR RefSeq; WP_002852601.1; NZ_SZUC01000001.1.
DR RefSeq; YP_002344169.1; NC_002163.1.
DR AlphaFoldDB; Q0PAC8; -.
DR IntAct; Q0PAC8; 38.
DR STRING; 192222.Cj0762c; -.
DR PaxDb; 192222-Cj0762c; -.
DR EnsemblBacteria; CAL34890; CAL34890; Cj0762c.
DR GeneID; 905072; -.
DR KEGG; cje:Cj0762c; -.
DR PATRIC; fig|192222.6.peg.750; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_7; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAL34890.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000799};
KW Transferase {ECO:0000313|EMBL:CAL34890.1}.
FT DOMAIN 30..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 389 AA; 43185 MW; 8CB7788C0E2F46B6 CRC64;
MLTKRSQVLE ESITLAITAL ANELKAKGED IISFSAGEPD FDTPQTIKNA AISAIEKGCG
KYTAVAGIPE VLKAIQTKFK KDNNLDYETN EIITNVGAKH SLFECIECLV EKDDEVIIPS
PYWVSYPEMV KFAGGKPVFI EGLEENGFKI TAEQLKKAIT AKTKVLMLNS PSNPVGSIYS
KEELTQIAKV LEGTQITVLS DEMYEKLRYD GFDFVAFASV SKDALKRTVT INGLSKCGAM
PGWRFGYMAS KNKALISAVK RLQGQSTSNI CSITQHAAIP ALNGECDKDI EKMRQAFEKR
RNLALDILKQ IPNISVYKPE GAFYLFVNIQ KIEKDSMKFC QKLLEQEKVA VVPGVGFGMD
GYFRLSYATS DELIKKGLER IANFIKNYK
//
