ID B1I8U7_STRPI Unreviewed; 404 AA.
AC B1I8U7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN OrderedLocusNames=SPH_2136 {ECO:0000313|EMBL:ACA37148.1};
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214 {ECO:0000313|EMBL:ACA37148.1, ECO:0000313|Proteomes:UP000002163};
RN [1] {ECO:0000313|Proteomes:UP000002163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6 {ECO:0000313|Proteomes:UP000002163};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000936; ACA37148.1; -; Genomic_DNA.
DR RefSeq; WP_000666465.1; NC_010380.1.
DR AlphaFoldDB; B1I8U7; -.
DR GeneID; 66807057; -.
DR KEGG; spv:SPH_2136; -.
DR HOGENOM; CLU_017584_4_2_9; -.
DR OMA; CALDLCI; -.
DR Proteomes; UP000002163; 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; 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:ACA37148.1};
KW Transferase {ECO:0000313|EMBL:ACA37148.1}.
FT DOMAIN 34..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 404 AA; 45776 MW; 6088F5C94EA033CC CRC64;
MKEYNKSSKL EHVAYDIRGP VLEEAMRMRA NGEKILRLNT GNPAEFGFTA PDEVIHDLIM
NARDSEGYSD SKGIFSARKA IMQYCQLKKF PNVDIDDIYL GNGVSELIVM SMQGLLDNGD
EVLVPMPDYP LWTAAVSLAG GNAVHYICDE AVEWYPDIDD IKSKITSNTK AIVLINPNNP
TGALYPKEFL LEIIEIARQN DLIIFADEIY DRMVMDGHVH TPVASLAPDV FCVSMNGLSK
SHRIAGFRVG WMVLSGPKTH VKGYIEGLNM LSNMRLCSNV LAQQVVQTSL GGHQSVDELL
LPGGRIYEQR NFIYNAIQDI PGLSAVKPKA GLYIFPKIDR NMYRIDDDEQ FVLDFLKQEK
VLLVHGRGFN WQEPDHFRIV YLPRVDELAQ IQEKMTRFLK QYRR
//