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Database: UniProt
Entry: G6B031_9BACT
LinkDB: G6B031_9BACT
Original site: G6B031_9BACT 
ID   G6B031_9BACT            Unreviewed;       392 AA.
AC   G6B031;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Aminotransferase, class I/II {ECO:0000313|EMBL:EHJ37987.1};
GN   ORFNames=HMPREF0673_02248 {ECO:0000313|EMBL:EHJ37987.1};
OS   Leyella stercorea DSM 18206.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Leyella.
OX   NCBI_TaxID=1002367 {ECO:0000313|EMBL:EHJ37987.1, ECO:0000313|Proteomes:UP000004407};
RN   [1] {ECO:0000313|EMBL:EHJ37987.1, ECO:0000313|Proteomes:UP000004407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18206 {ECO:0000313|EMBL:EHJ37987.1,
RC   ECO:0000313|Proteomes:UP000004407};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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:EHJ37987.1}.
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DR   EMBL; AFZZ01000193; EHJ37987.1; -; Genomic_DNA.
DR   AlphaFoldDB; G6B031; -.
DR   PATRIC; fig|1002367.3.peg.1811; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_3_10; -.
DR   Proteomes; UP000004407; 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:EHJ37987.1};
KW   Transferase {ECO:0000313|EMBL:EHJ37987.1}.
FT   DOMAIN          23..374
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   392 AA;  44209 MW;  1B6C6497C01E5D5C CRC64;
     MPESPIRKLA PLAVDAKKRG VKVYHLNIGQ PDLPTPEVGL DALKHIDRSV LEYSPSQGYY
     SYRERLTGYY KRFNINVSPD DIIITAGGSE AVLFAFMSCL NPGDEIIIPE PAYANYMAFA
     ISAGAKIRTI ATTIEEGFSL PKVEKFEELI NERTRAILIC NPNNPTGYLY TRREMNQIRD
     LVKKYDLYLF SDEVYREYIY TGSPYISACH LEGIEDNVIL IDSVSKRYSE CGIRIGALIT
     KNSQVRAAVM KLCQARLSPP LLGQIVADAS LDAPEDYYRD VYEEYVERRK CLIDGLNRIP
     GVYSPIPMGA FYTVAKLPVD DSEKFCRWCL EEFQYEGETI MMAPAAGFYT TPGAGINQVR
     IAYVLKKDDL ERALIVLRKA LEAYPGRVDS ND
//
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