NOAT_STRMU
ID NOAT_STRMU Reviewed; 393 AA.
AC Q8DTM1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Asparagine--oxo-acid transaminase {ECO:0000303|PubMed:22569339};
DE EC=2.6.1.14 {ECO:0000269|PubMed:22569339};
DE AltName: Full=Asparagine:2-oxoglutarate aminotransferase {ECO:0000305|PubMed:22569339};
GN Name=aspB {ECO:0000312|EMBL:AAN58989.1};
GN OrderedLocusNames=SMU_1312 {ECO:0000312|EMBL:AAN58989.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 25175 / DSM 20523 / JCM 5705 / NBRC 13955 / NCIMB 702062 / NCTC
RC 10449;
RX PubMed=22569339; DOI=10.1038/msb.2012.13;
RA Yamada T., Waller A.S., Raes J., Zelezniak A., Perchat N., Perret A.,
RA Salanoubat M., Patil K.R., Weissenbach J., Bork P.;
RT "Prediction and identification of sequences coding for orphan enzymes using
RT genomic and metagenomic neighbours.";
RL Mol. Syst. Biol. 8:581-581(2012).
CC -!- FUNCTION: Catalyzes the transamination reaction between L-asparagine
CC and 2-oxoglutarate to produce L-glutamate and 2-oxosuccinamate
CC (PubMed:22569339). Is not active with pyruvate as amine acceptor
CC (PubMed:22569339). May also use other amino acids as substrates.
CC {ECO:0000269|PubMed:22569339, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-asparagine = 2-oxosuccinamate + an L-
CC alpha-amino acid; Xref=Rhea:RHEA:19813, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:57735, ChEBI:CHEBI:58048, ChEBI:CHEBI:59869; EC=2.6.1.14;
CC Evidence={ECO:0000269|PubMed:22569339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-asparagine = 2-oxosuccinamate + L-
CC glutamate; Xref=Rhea:RHEA:52528, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57735, ChEBI:CHEBI:58048; EC=2.6.1.14;
CC Evidence={ECO:0000269|PubMed:22569339};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|RuleBase:RU000481,
CC ECO:0000305|PubMed:22569339};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE014133; AAN58989.1; -; Genomic_DNA.
DR RefSeq; NP_721683.1; NC_004350.2.
DR RefSeq; WP_002263716.1; NC_004350.2.
DR AlphaFoldDB; Q8DTM1; -.
DR SMR; Q8DTM1; -.
DR STRING; 210007.SMU_1312; -.
DR PRIDE; Q8DTM1; -.
DR EnsemblBacteria; AAN58989; AAN58989; SMU_1312.
DR KEGG; smu:SMU_1312; -.
DR PATRIC; fig|210007.7.peg.1176; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_9; -.
DR OMA; SVAMTGW; -.
DR PhylomeDB; Q8DTM1; -.
DR BRENDA; 2.6.1.14; 14748.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0047297; F:asparagine-oxo-acid transaminase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Asparagine--oxo-acid transaminase"
FT /id="PRO_0000439796"
FT BINDING 39
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 176
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 370
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
SQ SEQUENCE 393 AA; 43501 MW; 3A81DC3F3124DFB2 CRC64;
MTKLSRRVLE MEESVTLATS ARAKTLKAQG RDVLELSLGQ PDFVTPKNIQ EAAMKSIRDG
RASFYTIASG LPELKDAISQ YFEKFYGYSV ERKQIVVGTG AKFILYALFA AVINPKDEVI
IPTPFWVSYA DQIKMNDGVP VFIRTSEENH FKATVEQLEA ARTNKTKMIV LNSPSNPTGM
IYSKKELEAI GNWAVKHDIL ILSDDIYGRL VYNGARFTPI STISQPICQQ TIVINGVSKT
YSMTGWRVGY AVGDPEIIGA MSKIVSQTTS NLTTAAQYAA IEALIGNQDT VEVMRQAFEE
RLNTIYPLLA KVPGFHVVKP EGAFYFFPNV KKAMEMKGYT DVTEFTTALL EETGVALVTG
AGFGAPENVR LSYATDMVTL KEAINRIQAF MEK
