ID K2CX60_9BACT Unreviewed; 326 AA.
AC K2CX60;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
DE Flags: Fragment;
GN ORFNames=ACD_41C00190G0002 {ECO:0000313|EMBL:EKD79019.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD79019.1};
RN [1] {ECO:0000313|EMBL:EKD79019.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD79019.1}.
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DR EMBL; AMFJ01017072; EKD79019.1; -; Genomic_DNA.
DR AlphaFoldDB; K2CX60; -.
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..326
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT NON_TER 326
FT /evidence="ECO:0000313|EMBL:EKD79019.1"
SQ SEQUENCE 326 AA; 36065 MW; CA21E18936099A65 CRC64;
MLNFAQRISR LGTEQAFHVL ARAKQAEREG RDMIHMEIGD TDFQTPQPIV EAAIQALRDN
KTKYLPSAGL MELREVLAEQ MSTSRGISAK PEEMIVTPGG KPMIFYTLLA LVNEGDEVIY
PNPGFPTYES VINFIGAKPV ALEMNGENGF NFDIAELKRL ANSKTKLIIV NSPQNPTGGI
LTHESLEAIV EVAKQNDAWI FADEVYSELV FEGKFESILS IPGARERTIV LDAYTKTFSM
SGWRCGYGLC PTKEMADVIA NLINNSVSCA ANFTQWAGIA AWKDPAMPQA VADMREELRK
RRDVLYAGLE NLEGVSCHLP QGAIYL
//
