ID Q182A9_CLOD6 Unreviewed; 402 AA.
AC Q182A9;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Pyridoxal phosphate-dependent transferase {ECO:0000313|EMBL:CAJ69309.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CAJ69309.1};
GN OrderedLocusNames=CD630_24240 {ECO:0000313|EMBL:CAJ69309.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ69309.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ69309.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ69309.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; AM180355; CAJ69309.1; -; Genomic_DNA.
DR RefSeq; WP_004454722.1; NZ_JAUPES010000003.1.
DR RefSeq; YP_001088936.1; NC_009089.1.
DR AlphaFoldDB; Q182A9; -.
DR STRING; 272563.CD630_24240; -.
DR EnsemblBacteria; CAJ69309; CAJ69309; CD630_24240.
DR GeneID; 66354819; -.
DR KEGG; cdf:CD630_24240; -.
DR KEGG; pdc:CDIF630_02666; -.
DR PATRIC; fig|272563.120.peg.2558; -.
DR eggNOG; COG1167; Bacteria.
DR OrthoDB; 9802328at2; -.
DR PhylomeDB; Q182A9; -.
DR BioCyc; PDIF272563:G12WB-2575-MONOMER; -.
DR Proteomes; UP000001978; Chromosome.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42790:SF19; AROMATIC AMINO ACID AMINOTRANSFERASE DDB_G0272014; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:CAJ69309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001978};
KW Transferase {ECO:0000313|EMBL:CAJ69309.1}.
FT DOMAIN 44..387
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 402 AA; 45304 MW; 1A7879BF96F39A6C CRC64;
MKYAKRMDMV KASAIRDSQK KIAQKVASGG TVISFAAGLP DPNLFPIEEI SEITQKVLNE
RGKFALAYGP TKGEDELLDL LVKRMKEEEN IDTKAENIII TTGSQQGIAL SAMILLEKGD
VVVTENPSYL GAINAFRPYE CDFLGVDTDE EGMVTDDLDK LLSENSNIKV IYVIPTFQNP
TGKTWSLQRR KDFMEVVNKY DVIVIEDNPY GEIRFTPEPL PTLKSLDTKD KVLYLGSFSK
VLCPGFRVAW MCGNVDIIDK AELLKQGIDL QSNQFSQVQV IEFLKKYNLN EHIEKIRAEY
KKRCLLMLDA MKKHFPEEAK YTEPDGGMFI WVELPESINV DDLLDKAIDA GVAYVSGESF
FANNGPKNTM RLNYTTMSEE QIVKGVEILA EVIKKELNYA CE
//
