ID A0A0G1PCK0_9BACT Unreviewed; 369 AA.
AC A0A0G1PCK0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Methionine aminotransferase {ECO:0000313|EMBL:KKT94059.1};
GN ORFNames=UW94_C0002G0033 {ECO:0000313|EMBL:KKT94059.1};
OS Parcubacteria group bacterium GW2011_GWA2_45_14.
OC Bacteria.
OX NCBI_TaxID=1618832 {ECO:0000313|EMBL:KKT94059.1, ECO:0000313|Proteomes:UP000034475};
RN [1] {ECO:0000313|EMBL:KKT94059.1, ECO:0000313|Proteomes:UP000034475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT94059.1}.
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DR EMBL; LCKH01000002; KKT94059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1PCK0; -.
DR STRING; 1618832.UW94_C0002G0033; -.
DR Proteomes; UP000034475; 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; 3.40.640.10; 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 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:KKT94059.1};
KW Transferase {ECO:0000313|EMBL:KKT94059.1}.
FT DOMAIN 20..364
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 369 AA; 41496 MW; 03E1BBDA9D7E50A9 CRC64;
MTQQLGIREL AERAKKEGAI DLAQGVIDTD LPTPLVNALH KVPIQKISRY DNKRGVPAYR
EALVNYLGSR GWNIEVDNVM SVAGAMAGIT SSLLTDLKPG TKVLLPEPFY IVHEILLNAL
GFEIVFLPAK IGEQLDWDDV IDKMDDVDGV IITSPANPTG QTASLETLKK LSEAARDKNC
LLVLDEMYRE FIWDNPPKDD ADYQKMDWSK TVLVRSWSKA FAIPGWRVGF SVTSPERIEE
MAVRHDALYI GGSTVSQHVL AEVLQNNLPE LNQYVVELRE MLLRNKAVLE EAFTKYGFIP
QPVPATYYML MKHDRPTDMA VVEELIAKKI VTTPATIFFH DRSKETGFLR IHFAAKEEAA
RKVAEILMK
//