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Database: UniProt
Entry: D5Q5Y7_CLODI
LinkDB: D5Q5Y7_CLODI
Original site: D5Q5Y7_CLODI 
ID   D5Q5Y7_CLODI            Unreviewed;       398 AA.
AC   D5Q5Y7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=HMPREF0220_2319 {ECO:0000313|EMBL:EFH06609.1};
OS   Clostridioides difficile NAP08.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=525259 {ECO:0000313|EMBL:EFH06609.1, ECO:0000313|Proteomes:UP000003227};
RN   [1] {ECO:0000313|EMBL:EFH06609.1, ECO:0000313|Proteomes:UP000003227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAP08 {ECO:0000313|EMBL:EFH06609.1,
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|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC       ECO:0000256|RuleBase:RU000481}.
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:EFH06609.1}.
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DR   EMBL; ADNX01000054; EFH06609.1; -; Genomic_DNA.
DR   RefSeq; WP_003419570.1; NZ_GG770713.1.
DR   AlphaFoldDB; D5Q5Y7; -.
DR   HOGENOM; CLU_017584_4_3_9; -.
DR   Proteomes; UP000003227; Unassembled WGS sequence.
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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:EFH06609.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EFH06609.1}.
FT   DOMAIN          32..383
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   398 AA;  44637 MW;  68F4ECCF1EA71858 CRC64;
     MNYSNRVSAM QASPIRKLVP FAQAAKDKGI KVYHLNIGQP DIKTPKGFFD AVKNFDSEVL
     EYATSEGIPE LLEALQNYYK TYNMNFEKDE LLVTNGGSEA LLFTMMAVCD PGDNLLVPEP
     FYTNYNGFGQ SVNVEVNAVT TKAENGFHLP SKEEILSKVD DKTKAIILSN PGNPTGAIYT
     KEELNILAEI AKEKDLWIIA DEVYREFVYD GLEYTSCGNL EGVQDRVIII DSVSKRYSAC
     GARIGSIACK NKGLIAQILK LCQGRLCVPT LEQIGAVELY KTPVSYFKEV NEEYKKRRDV
     LYNELMKVEG VICKKPTGAF YIVAKLPVEN AEDFTIWMLK EFNKDNETVM VCPAEGFYAT
     PGLGRDEIRL AYILNEKDLH RAATLLKEGL EQYVALQK
//
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