ID R5U923_9BACE Unreviewed; 399 AA.
AC R5U923;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=BN535_00896 {ECO:0000313|EMBL:CCZ74668.1};
OS Bacteroides caccae CAG:21.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ74668.1, ECO:0000313|Proteomes:UP000017990};
RN [1] {ECO:0000313|EMBL:CCZ74668.1, ECO:0000313|Proteomes:UP000017990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:21 {ECO:0000313|Proteomes:UP000017990};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCZ74668.1}.
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DR EMBL; CBAN010000185; CCZ74668.1; -; Genomic_DNA.
DR AlphaFoldDB; R5U923; -.
DR Proteomes; UP000017990; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
FT DOMAIN 32..384
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 399 AA; 44653 MW; 5E62C63FEED7EFB9 CRC64;
MPTISIRGNE MPASPIRKLA PLADAAKQRG VHVFHLNIGQ PDLPTPQVAI DAIRNIDRKV
LEYSPSAGYR SYREKLVGYY AKFNINLTAD DIIITSGGSE AVLFSFLSCL NPGDEIIVPE
PAYANYMAFA ISAGAKIRTI ATTIEEGFSL PKVEKFEELI NERTKAILIC NPNNPTGYLY
TRREMNQIRD LVKKYDLFLF SDEVYREFIY TGSPYISACH LEGIENNVVL IDSVSKRYSE
CGIRIGALIT KNKEIRDAVM KFCQARLSPP LIGQIAAEAS LDAPEEYSRE TYDEYVERRK
CLIDGLNRIP GVYSPIPMGA FYTVAKLPVD DSDKFCAWCL SDFEYEGQTV FMAPASGFYT
TPGSGINEVR IAYVLKKEDL TRALFVLQKA LEAYPGRTE
//