ID A0A139NN33_9STRE Unreviewed; 388 AA.
AC A0A139NN33;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=STRDD13_01639 {ECO:0000313|EMBL:KXT77263.1};
OS Streptococcus sp. DD13.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT77263.1, ECO:0000313|Proteomes:UP000070387};
RN [1] {ECO:0000313|EMBL:KXT77263.1, ECO:0000313|Proteomes:UP000070387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD13 {ECO:0000313|EMBL:KXT77263.1,
RC ECO:0000313|Proteomes:UP000070387};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) 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|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:KXT77263.1}.
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DR EMBL; LQRH01000063; KXT77263.1; -; Genomic_DNA.
DR RefSeq; WP_067103774.1; NZ_KQ969509.1.
DR AlphaFoldDB; A0A139NN33; -.
DR STRING; 1777881.STRDD13_01639; -.
DR PATRIC; fig|1777881.3.peg.1734; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000070387; 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: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:KXT77263.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070387};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KXT77263.1}.
FT DOMAIN 32..382
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 43204 MW; E31BD44B13BCE02B CRC64;
MDISHRFNKH LDKIKISMIR EFDQSISDIP GVLKLTLGEP DFSTPEHVQE AAKKAIDDGK
SHYTGMAGLL ELRQATASFM KEKYRVSYQA EDEILVTIGA TEALSASLIA ILEPGDTVLL
PAPAYPGYEP IVNMVGAEII EIDTTDNQFV LTPEALEEGI QEAGSSLKAV ILNYPANPTG
VTYSREQIAA FAKVIEKYPI FVVSDEVYSE LTYTDEDHTS IAEFLPTQTI LVQSLSKSHA
MTGWRLGFIL SSKEIIAQIV KSHQYLVTAA TTLVQYAGVE ALANGKDDAL PMREEYRERR
DYILEQMTKL GFSIIKPDGA FYIFARIPEG YNQNSFEFLQ DFAQQQAVAF IPGAAFGKYG
EGYVRVSYAA SMETIQEAMR RLAVFMRR
//
