ID G5STJ8_9BACT Unreviewed; 394 AA.
AC G5STJ8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF9441_02703 {ECO:0000313|EMBL:EHG99440.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHG99440.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHG99440.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHG99440.1,
RC ECO:0000313|Proteomes:UP000003598};
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 (MAR-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 ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:EHG99440.1}.
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DR EMBL; AFFY01000044; EHG99440.1; -; Genomic_DNA.
DR RefSeq; WP_008621392.1; NZ_JH376615.1.
DR AlphaFoldDB; G5STJ8; -.
DR STRING; 762968.HMPREF9441_02703; -.
DR GeneID; 78583583; -.
DR PATRIC; fig|762968.3.peg.2404; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_10; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000003598; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:EHG99440.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 39..390
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 44934 MW; 1E7C5D8C5BA51E2C CRC64;
MEDKLYNFRI QPAERLSSVQ EYYFSVKLKE VARMNAEGKD IISLAIGSPD MPPSPQTIET
LCEEARHADA HGYQPTTGIP ELRRAMAEFY KRWYDVDLDP ACEIQPLIGS KEGILHVTLA
LANPGDRVLV PNPGYPTYTS LSKILGQRIT YYDLLPENGW QPDFKALEEM DLTGVKIMWT
NYPNMPTGAN ARRETYEKLV DFALRHNLVI VNDNPYSFIL NHERLSILQV PGAKRCCIEF
NSMSKSHNMP GWRVGMLATN AEFVKWILKV KSNIDSGTFR PMQLAAAAAY RNDAQWHEEA
NIHVYAERRA LAEEIMYTLG CTFDPTQVGM FLWGRIPESC DNVEQLTEKI LHEARVFITP
GFIFGSNGSR YIRISLCAKK EKIAEALERI RKVF
//
