ID U2T0Z8_9FUSO Unreviewed; 397 AA.
AC U2T0Z8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF1984_00611 {ECO:0000313|EMBL:ERK68402.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK68402.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK68402.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK68402.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERK68402.1}.
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DR EMBL; AWVR01000017; ERK68402.1; -; Genomic_DNA.
DR AlphaFoldDB; U2T0Z8; -.
DR STRING; 1321779.HMPREF1984_00611; -.
DR PATRIC; fig|1321779.3.peg.597; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_0; -.
DR Proteomes; UP000016640; 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; PTHR46383:SF4; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
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:ERK68402.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016640};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ERK68402.1}.
FT DOMAIN 44..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 45289 MW; 0695CFAA0BF62C24 CRC64;
MIEYRNNSIL TMKGKIMYIN KIVKEIQISD IRKIYEKMQT YDNAINMSIG EPDIDVPEEV
KEAVAYHAVN TRIKYSPVGG MPELRKKIAD FYNDNFNGNF SLDNVLVTVG STEGLGSVMK
AIIAEGDEVL MPTPAYVGYG SLIKLTGGEP KYIDLRENEF KLTAEILEKH ITPKTKLIIL
TNPNNPSGTT LPKEEMEKIA DLLKDKEIYL LSDEIYASIV FEEYTSFAEY WEKLEKQLII
VSGFSKSHSM TGYRIGYIIT NPELQLQVKK VSQYNVTSTS TLSQYGAMAA LEKCSDRREV
SEIYRKRIDY FKNELEKMGF KCLEPKGAFY IFAGYENIDR LQNMKSLDFA LDLLEKTGLA
IVPGSTFQVE GYVRFSIVHD IPILEEAIER LKKYMNL
//
