ID C4IDS0_CLOBU Unreviewed; 397 AA.
AC C4IDS0;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspB {ECO:0000313|EMBL:EEP55438.1};
GN ORFNames=CLP_3500 {ECO:0000313|EMBL:EEP55438.1};
OS Clostridium butyricum E4 str. BoNT E BL5262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP55438.1, ECO:0000313|Proteomes:UP000003081};
RN [1] {ECO:0000313|EMBL:EEP55438.1, ECO:0000313|Proteomes:UP000003081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.;
RL Submitted (AUG-2009) 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:EEP55438.1}.
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DR EMBL; ACOM01000004; EEP55438.1; -; Genomic_DNA.
DR RefSeq; WP_003408961.1; NZ_ACOM01000004.1.
DR AlphaFoldDB; C4IDS0; -.
DR STRING; 1492.ATN24_04810; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_9; -.
DR Proteomes; UP000003081; 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 PRINTS; PR00753; ACCSYNTHASE.
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:EEP55438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003081};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EEP55438.1}.
FT DOMAIN 31..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 44102 MW; 4660B90A1C70A0E1 CRC64;
MNLSKKAGNI SPSITLSITA KANELKAQGV DVVSFGAGEP DFNTPQNIIN SAIKAMQDGK
TKYTPAGGIL ELKKTICKKF KEDNGLDYTT DQITISTGAK QCLANVFMAI LNPGDEILIP
IPYWVSYPEL VKLADGVPVF VETLKENNYK YTIEDLEKAV SDKTKVILIN SPNNPTGTIY
NREELIEIAE FAKKHDLLII SDEIYEKLIY DGEKHISIAS LSEDAFERTV VINGVSKTYA
MTGWRLGYMA ASKEITKLMT SIQSHMTSNV NTIAQYAAIE ALNGPIEDLN TMVKEFERRR
NFMVDRLSKI DGVSIIKPSG AFYIMVNISS YFNTTFKGEE IKNSLDFSRV LLDEEKVAVI
PGAGFGLDEY IRLSYATSMD IIETGIDRIA MFINKIK
//
