ID A0A0M2U5X9_9FIRM Unreviewed; 451 AA.
AC A0A0M2U5X9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:KKM10161.1};
GN ORFNames=SY88_15980 {ECO:0000313|EMBL:KKM10161.1};
OS Clostridiales bacterium PH28_bin88.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM10161.1, ECO:0000313|Proteomes:UP000034222};
RN [1] {ECO:0000313|EMBL:KKM10161.1, ECO:0000313|Proteomes:UP000034222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Robbins S., Tyson G.;
RT "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KKM10161.1}.
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DR EMBL; LAKY01000055; KKM10161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2U5X9; -.
DR STRING; 1605376.SY88_15980; -.
DR PATRIC; fig|1605376.3.peg.1368; -.
DR Proteomes; UP000034222; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KKM10161.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000034222};
KW Transferase {ECO:0000313|EMBL:KKM10161.1}.
SQ SEQUENCE 451 AA; 49901 MW; 3DFFC3F162F10ABA CRC64;
MIDRDRLKAL LKKELKRFED THPKSKEMFQ RAQASLLDGV PMNWMVRWAG GFPVFVKEGS
GAYFYDVDGN RYIDFCLGDT GAMTGHAPEG AVDAINARIK NGVTFMLPTE DAIWVGEELA
RRFGLPYWQV AISATDANRF SLRLARHITK RKYILVFNYC YHGTVDETFI SINEGVPGSR
RGNIGPQVNP VKTTKVIEFN DIAALEKALQ PEDVAAVLAE PAMTNIGIIH PDPGYHEALR
EITSRTGTLL IIDETHTMCT GPGGYTKAYG LKPDMLTVGK AIGGGIPTAV YGFSREVADR
IRGTIELEQA DVGGIGGTLA GNALSMAAMR ATLENVLTKE AYDRNTALAQ RFEEGLQSVI
DEKKLPWIVK RLGCRVEYWF HPTPPRNGGE AAAAVDPELD RYMHLTALNR GILMTPFHNM
ALICAQTTQE DIDYHTNVFS ESVEMLIGER D
//
