ID B9DVH7_STRU0 Unreviewed; 404 AA.
AC B9DVH7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN OrderedLocusNames=SUB1529 {ECO:0000313|EMBL:CAR43275.1};
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR43275.1, ECO:0000313|Proteomes:UP000000449};
RN [1] {ECO:0000313|Proteomes:UP000000449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR43275.1; -; Genomic_DNA.
DR RefSeq; WP_015911837.1; NC_012004.1.
DR AlphaFoldDB; B9DVH7; -.
DR STRING; 218495.SUB1529; -.
DR KEGG; sub:SUB1529; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_2_9; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000000449; 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:CAR43275.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000449};
KW Transferase {ECO:0000313|EMBL:CAR43275.1}.
FT DOMAIN 34..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 404 AA; 45605 MW; D0112A35E61118D4 CRC64;
MKIFEKSSKL EHVAYDIRGP VLEEAERMMA NGEKILRLNT GNPAAFGFEA PDEVIRDLIL
NARNSEGYSD SRGIFSARKA IMQYCQLKDF PEVDINDIYL GNGVSELISM SMQALLDDGD
EVLVPMPDYP LWTACVSLAG GKAVHYICDE QAEWYPDIDD IKSKVTDRTK AIVIINPNNP
TGALYPKELL EEIVDIAREH QLIIFADEIY DRLVMDGGKH IAIASLAPDV FCVSMNGLSK
SHRIAGFRVG WMVLSGPKNH VKGYIEGLNM LANMRLCSNV LAQQVVQTSL GGHQSVDDLL
LPGGRIFEQR NFIHKAINDI PGLSAVKPKA GLYIFPKIDR QMYRIDDDEQ FVLDLLKQEK
VMLVHGRGFN WKDPDHFRIV YLPRVEELAD VQEKITRVLK QYKR
//
