ID K2D3N6_9BACT Unreviewed; 429 AA.
AC K2D3N6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=ACD_39C01953G0001 {ECO:0000313|EMBL:EKD81139.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD81139.1};
RN [1] {ECO:0000313|EMBL:EKD81139.1}
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:EKD81139.1}.
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DR EMBL; AMFJ01016375; EKD81139.1; -; Genomic_DNA.
DR AlphaFoldDB; K2D3N6; -.
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 35..396
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 429 AA; 48215 MW; 322BE2010B0AE3DF CRC64;
MFADRYADRV QFLSPSSIRK MMAIAKDLIA HGKTVYELNI GQPDIECIPE FAEAIEKKAR
TGQINYSPII GEKYLRETYA RYLNNFFDHD GKPHLVIDTE NVLVTVGASH ALTSCFLGIC
NPGDEVLVIE PYFSPYTGFL AVAGGKLRAI PTRAEDDFAL PPAEEIAKLI TPKTRAIIFN
SPNNPSGKIY SAEEVERLAR ICVEHNLFLI SDEVYREMTL GDKEAFSVLQ VDFGNEEMNE
KLKNAIIMID SASKTFSLCG VRIGFLVARQ PILEKLALVV AHTTACVSDI MQYGVAWAYD
AILSRPDYVE QMRRIYHERL EATMEAIAEY LPGVVAPKPD GAFYLMLKFP EFEDITEFCH
FMLEKFNLGN ETVAVTPAGS FYLTPGRGRN EIRIALVVGP DKMRRSIQII SEALKAFRQF
KVNLVRPML
//
