ID D5Q0X3_CLODI Unreviewed; 365 AA.
AC D5Q0X3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:EFH08415.1};
GN ORFNames=HMPREF0220_0555 {ECO:0000313|EMBL:EFH08415.1};
OS Clostridioides difficile NAP08.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=525259 {ECO:0000313|EMBL:EFH08415.1, ECO:0000313|Proteomes:UP000003227};
RN [1] {ECO:0000313|EMBL:EFH08415.1, ECO:0000313|Proteomes:UP000003227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP08 {ECO:0000313|EMBL:EFH08415.1,
RC ECO:0000313|Proteomes:UP000003227};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (MAY-2010) 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};
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:EFH08415.1}.
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DR EMBL; ADNX01000015; EFH08415.1; -; Genomic_DNA.
DR RefSeq; WP_003418382.1; NZ_GG770712.1.
DR AlphaFoldDB; D5Q0X3; -.
DR HOGENOM; CLU_027686_3_1_9; -.
DR Proteomes; UP000003227; 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; 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; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EFH08415.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:EFH08415.1}.
FT DOMAIN 20..286
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 336
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 365 AA; 41314 MW; EDABCA56096D6A6D CRC64;
MKKTYLFSPG PVMVTDKVRN SLLHYDICHR GNEFMDLFKD TQQKINKLYN ATSNYYSLIV
SGSGTSVNEC VLSSIFDKED AVLLVSNGVF GERLEEILST YNVKTYKPNF EWAEYPDLNI
LEKYIIEHSD IKVIAMVFHE TSSGMINPVP ELGKLAKKYN KIFFVDAISA SAGEYIDVEE
FNIDIITGVG GKALGAFPGS AYLCAKESIL QDIKENQCKN VYLNLYKHYK VAKSSSQTPN
TPNVTLIFAL NEALTEFLED DSKIERYKEC SAILRNGMEE LGLTFLLPDK YMSNTVTSVF
LPKEINVDEF ILGLERESGY VVYPGKGKFL DANIFQVANM GEIYPEDCYK FLDILKSRLE
IKKVI
//
