ID A0A1B7LI45_9FIRM Unreviewed; 381 AA.
AC A0A1B7LI45;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Class V aminotransferase {ECO:0000313|EMBL:OAT86089.1};
GN ORFNames=A6M21_03975 {ECO:0000313|EMBL:OAT86089.1};
OS Desulfotomaculum copahuensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1838280 {ECO:0000313|EMBL:OAT86089.1, ECO:0000313|Proteomes:UP000078532};
RN [1] {ECO:0000313|EMBL:OAT86089.1, ECO:0000313|Proteomes:UP000078532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMa1 {ECO:0000313|EMBL:OAT86089.1,
RC ECO:0000313|Proteomes:UP000078532};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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:OAT86089.1}.
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DR EMBL; LYVF01000040; OAT86089.1; -; Genomic_DNA.
DR RefSeq; WP_066666393.1; NZ_LYVF01000040.1.
DR AlphaFoldDB; A0A1B7LI45; -.
DR STRING; 1838280.A6M21_03975; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000078532; Unassembled WGS sequence.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OAT86089.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000078532};
KW Transferase {ECO:0000313|EMBL:OAT86089.1}.
FT DOMAIN 6..326
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 381 AA; 40546 MW; BC7989B3CC33FB73 CRC64;
MQDKHYLMIP GPTPVPPAVV AAMSRPMIGH RSEDFAALHR RIEEKIRRVF GTVHEVFILT
HSGTGGLETA IANVVSPGDK VLALITGNFG ERFAKIARAY GAEVDEINFG WGKNVDLTVV
AEKLAGDPGY KAVLATQNET STGVLNDIAG IGALVAKTPA LLLVDGVSGV GGIEIKMDEW
HVDILVTASQ KAMMLPPGLA MVAVGPKAWP VIEGNSAPRF YFSLPAARKS FEKWNTAYTP
NVSLFQGLDA ALDMMLAEGL ENVYARHILL ARAVREAVLA LGLRPLAEAG YASPTVTSVY
SPEGIGADDI RKVLKEELGV TFAGGQGILK GKIFRIAHMG FADKMDVILA VAALEMALTR
VGYPVELGKG VKAAQEVLLG R
//
