ID B1BX22_CLOPF Unreviewed; 380 AA.
AC B1BX22;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:EDT13766.1};
GN ORFNames=AC3_1033 {ECO:0000313|EMBL:EDT13766.1};
OS Clostridium perfringens E str. JGS1987.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=451755 {ECO:0000313|EMBL:EDT13766.1, ECO:0000313|Proteomes:UP000005337};
RN [1] {ECO:0000313|EMBL:EDT13766.1, ECO:0000313|Proteomes:UP000005337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E str. JGS1987 {ECO:0000313|Proteomes:UP000005337};
RA Paulsen I., Sebastian Y.;
RT "Annotation of Clostridium perfringens E str. JGS1987.";
RL Submitted (JUL-2007) 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:EDT13766.1}.
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DR EMBL; ABDW01000038; EDT13766.1; -; Genomic_DNA.
DR RefSeq; WP_003465877.1; NZ_ABDW01000038.1.
DR AlphaFoldDB; B1BX22; -.
DR Proteomes; UP000005337; 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:EDT13766.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:EDT13766.1}.
FT DOMAIN 35..289
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 192
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 380 AA; 42991 MW; 422AFDB182DD5B25 CRC64;
MNCNKTIYTP GPTNLRENVR RARALKTTNP DVDLDFVEFY KETCDRFGEI INTKNDCYIL
SGEGILGLEA ACASLTEKGD KVLVLDNGLY GRWFDGFVNM YGGEVTYFSG DYTKEIDVEA
LSKFLEKNND FKYATVVHCD TPTGVLNPVD KICPLLKSYG ILTVVDSVSA MLGEEFKVDE
WQIDIALGGS QKVFSAEPGL TMLSISDDAR KVMENRETPI VGFYCNLNIW KNYYKDKWFP
YTMPTSDIIS LRVAIDNILE EGKEKVIERH RKIGEATRKA VKEYGLDLFL KNGYSNTVTA
VEIPEEIGAL NLRNHLNKKY NVLMSTSLDK YEDKLLRIGH MGENANIEDI TYVLNAIDKA
LKDLGFSSEK QLDKLFIENI
//
