ID A3CJY7_STRSV Unreviewed; 390 AA.
AC A3CJY7;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspC {ECO:0000313|EMBL:ABN43492.1};
GN OrderedLocusNames=SSA_0023 {ECO:0000313|EMBL:ABN43492.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN43492.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN43492.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN43492.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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|RuleBase:RU000481}.
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DR EMBL; CP000387; ABN43492.1; -; Genomic_DNA.
DR RefSeq; WP_011836286.1; NC_009009.1.
DR RefSeq; YP_001034042.1; NC_009009.1.
DR AlphaFoldDB; A3CJY7; -.
DR STRING; 388919.SSA_0023; -.
DR KEGG; ssa:SSA_0023; -.
DR PATRIC; fig|388919.9.peg.22; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_9; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000002148; 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; 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:SF4; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383; 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:ABN43492.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABN43492.1}.
FT DOMAIN 32..382
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 390 AA; 43169 MW; BA8A46E7A65B64C8 CRC64;
MDLSKKFNKN LGKIEISLIR QFDQSISAIP GVLRLTLGEP DFTTPDHIKE AAKAAIDANQ
SHYTGMSGLL ELRQAASSFV KEKYNLNYRP EDEVLVTIGA TEALSATLTA ILEEGDKVLL
PAPAYPGYEP IVNLVGAEIV EIDTTANNFV LTPEMLEAAI LEQGEQLKAV ILNYPANPTG
VTYSREQIKA LADVLGKYQV FVVCDEVYSE LTYTEQGHVS IAEYLPDQTI VINGLSKSHA
MTGWRLGFIF APAVFTAQLI KSHQYLVTAA NTMAQFAGIE ALTVGKDDAE PMKAEYIQRR
DYIIEKMAEL DFKIIKPDGA FYIFAKIPDG YNQDSFAFLQ DFAEKKAVAF IPGAAFGQYG
EGYIRLSYAA SMETIREALK RLKDYMEDYA
//
