ID Q5XAC2_STRP6 Unreviewed; 416 AA.
AC Q5XAC2;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN OrderedLocusNames=M6_Spy1506 {ECO:0000313|EMBL:AAT87641.1};
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636 {ECO:0000313|EMBL:AAT87641.1, ECO:0000313|Proteomes:UP000001167};
RN [1] {ECO:0000313|EMBL:AAT87641.1, ECO:0000313|Proteomes:UP000001167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394 {ECO:0000313|Proteomes:UP000001167};
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CP000003; AAT87641.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5XAC2; -.
DR KEGG; spa:M6_Spy1506; -.
DR HOGENOM; CLU_017584_4_2_9; -.
DR OMA; CALDLCI; -.
DR Proteomes; UP000001167; Chromosome.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AAT87641.1};
KW Transferase {ECO:0000313|EMBL:AAT87641.1}.
FT DOMAIN 46..406
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 416 AA; 46794 MW; 5BFFA631A9852BC4 CRC64;
MVYNMEYEVY ETMKIIEKSS KLEHVAYDIR GPVLDEANRM IASGEKILRL NTGNPAAFGF
EAPDEVIRDL IVNARLSEGY SDSKGIFSAR KAIMQYCQLK GFPDVDIEDI YLGNGVSELI
SMSLQALLDN GDEVLVPMPD YPLWTACVSL GGGKAVHYLC DEEAGWYPDI ADIKSKITSR
TKAIVVINPN NPTGALYPKE ILEDIVALAR EHQLIIFADE IYDRLVMDGK EHIAIASLAP
DVFCVSMNGL SKSHRIAGFR VGWMVLSGPK DHVKGYIEGL NMLANMRLCS NVLAQQVVQT
SLGGHQSVDA LLLPGGRIFE QRNFIYEAIN AIPGLSAVKP EAGLYLFPKI DRQMYRIDDD
EEFVLQLLKQ EKVMLVHGRG FNWKDPDHFR IVYLPSVEEL EDVQEKITRV LYQYRR
//