ID   B9D560_CAMRE            Unreviewed;       389 AA.
AC   B9D560;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Aminotransferase, class I/II {ECO:0000313|EMBL:EEF12859.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:EEF12859.1};
GN   ORFNames=CAMRE0001_1062 {ECO:0000313|EMBL:EEF12859.1};
OS   Campylobacter rectus RM3267.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF12859.1, ECO:0000313|Proteomes:UP000003082};
RN   [1] {ECO:0000313|EMBL:EEF12859.1, ECO:0000313|Proteomes:UP000003082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM3267 {ECO:0000313|EMBL:EEF12859.1,
RC   ECO:0000313|Proteomes:UP000003082};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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:EEF12859.1}.
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; ACFU01000035; EEF12859.1; -; Genomic_DNA.
DR   RefSeq; WP_002945763.1; NZ_ACFU01000035.1.
DR   AlphaFoldDB; B9D560; -.
DR   STRING; 553218.CAMRE0001_1062; -.
DR   eggNOG; COG0436; Bacteria.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000003082; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase 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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EEF12859.1};
KW   Transferase {ECO:0000313|EMBL:EEF12859.1}.
FT   DOMAIN          30..380
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   389 AA;  42515 MW;  4FEE02EE0A2EEAB5 CRC64;
     MLSKRVQVLG ESLTIEISTK AKEMKARGED VISFGAGEPD FDTPEIIKNE VKAALDKGCG
     KYTAVAGTPE VREAVAAKLK RDNGLNYAPN QIITNVGAKH SLFNVFQALV DHGDEVIVPS
     PYWVSYPEMV KFSGGNPVFI ETNEKTGFKI TPEQLKAAIT PRTKILVLNS PCNPTGAIYS
     RKELEALGEV LKDTKIIVAS DEMYEKLNYE GEFVATAAVS EDMFNRTITI NGLSKCGAMP
     GWRFGYMASP FKELNAAVNK LQSQSTSNIN SLTQAGAIPA LLGKADEDIA YMKGEFKKRR
     DLGVEMINAI PGLSVLKPDG AFYLFINCSE VEPDSMKFCK ELLEKAKVAV VPGVGFGMDG
     YFRLSFATDL ESIRKGIARI GEFVKSYKK
//