ID Q57R00_SALCH Unreviewed; 396 AA.
AC Q57R00;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspC {ECO:0000313|EMBL:AAX64861.1};
GN OrderedLocusNames=SCH_0955 {ECO:0000313|EMBL:AAX64861.1};
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX64861.1, ECO:0000313|Proteomes:UP000000538};
RN [1] {ECO:0000313|EMBL:AAX64861.1, ECO:0000313|Proteomes:UP000000538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67 {ECO:0000313|EMBL:AAX64861.1,
RC ECO:0000313|Proteomes:UP000000538};
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.Y., Wang H.S.,
RA Lee Y.S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; AE017220; AAX64861.1; -; Genomic_DNA.
DR RefSeq; WP_011264240.1; NC_006905.1.
DR AlphaFoldDB; Q57R00; -.
DR KEGG; sec:SCH_0955; -.
DR HOGENOM; CLU_032440_1_2_6; -.
DR Proteomes; UP000000538; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR000796; Asp_trans.
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; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
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:AAX64861.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AAX64861.1}.
FT DOMAIN 27..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 43537 MW; 891640CF0B8D02FB CRC64;
MFENITAAPA DPILGLADLF RADDRPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE
TTKNYLGIDG IPEFARCTQE LLFGKGSALI NDKRARTAQT PGGTGALRIA ADFLAKNTPV
KRVWVSNPSW PNHKSVFNAA GLEVREYAYY DAENHTLDFE ALQASLSEAQ AGDVVLFHGC
CHNPTGIDPT LEQWQVLAEL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAALHKELIV
ASSYSKNFGL YNERVGACTL VAADAETVDR AFSQMKSAIR ANYSNPPAHG ASIVATILSN
DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSY IIKQNGMFSF SGLTKDQVLR
LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL
//
