ID R6WSU2_9BACT Unreviewed; 395 AA.
AC R6WSU2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=BN673_01592 {ECO:0000313|EMBL:CDC97152.1};
OS Prevotella sp. CAG:474.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262926 {ECO:0000313|EMBL:CDC97152.1, ECO:0000313|Proteomes:UP000018116};
RN [1] {ECO:0000313|EMBL:CDC97152.1, ECO:0000313|Proteomes:UP000018116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:474 {ECO:0000313|Proteomes:UP000018116};
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 ECO:0000256|RuleBase:RU003693};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:CDC97152.1}.
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DR EMBL; CBGF010000008; CDC97152.1; -; Genomic_DNA.
DR AlphaFoldDB; R6WSU2; -.
DR STRING; 1262926.BN673_01592; -.
DR Proteomes; UP000018116; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd06454; KBL_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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693:SF3; LD36009P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000018116}.
FT DOMAIN 43..383
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 395 AA; 43976 MW; 41773BE607FBEB1F CRC64;
MGQLQERYKN YREPQKYMAA GVYPYFRAIT SKQGPEVEMD GHKVLMFGSN AYTGLTGDER
VIEAAHKALD KYGSGCAGSR FLNGTLDIHV QLEKELAEFE HKDDALCFAT GFSVNAGVIA
MVVGRGDYII CDDRDHASIV DGRRLSFATQ LHYKHNDMED LERVLQKLPK EAIKLIVVDG
VFSMEGDLAK LPEIVELKHK YNCSLMVDEA HGLGVFGKQG RGVCDHFGLT DEVDLIMGTF
SKSLASIGGF IAGDADTINF LRHSCRTYIF SASDTPAATA AALEALHILQ EEPSRLEHLW
DVTNYALKRF KEEGFEIGDT ESPIIPLYVR DIEKTFMVTK LAFDNGVFIN PVIPPACAPQ
DTLVRFALMA SHTQEQVERG VQILKKAFKE LEIIK
//
