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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//