ID   B0VR87_ACIBS            Unreviewed;       476 AA.
AC   B0VR87;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=ABSDF2181 {ECO:0000313|EMBL:CAP01506.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP01506.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAP01506.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAP01506.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAP01506.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VR87; -.
DR   KEGG; abm:ABSDF2181; -.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   BioCyc; ABAU509170:GCL9-1779-MONOMER; -.
DR   Proteomes; UP000001741; 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:CAP01506.1};
KW   Transferase {ECO:0000313|EMBL:CAP01506.1}.
FT   DOMAIN          107..468
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   476 AA;  53404 MW;  F8A794C7F38C6C96 CRC64;
     MSQKKSVLFQ QLLPVIKQYQ QSGFTHEKIV ELLKDQHDLN LVTVKTFKSY LYRYAKVNPA
     MSKNTATLQS MPTSREIKKS SKLEHVCYDI RGPVLRAANE MEEQGHKIIK LNIGNPAPFG
     FEAPQEIIND VALNLPNAIG YVDSKGIFPA RKAICQYYQQ KGILNMHVND VYIGNGVSEL
     IVMAMQGLLD DGDEMLIPMP DYPLWTAAVN LSGGTAIHYK CDEENSWYPD IADIESKITS
     NTRGIVIINP NNPTGSVYPR HVLEQIVALA KKHDLILFAD EIYDKIVYDG IEHVAVASLA
     GDQLCISFNG LSKAYRIAGF RSGWMAITGD KSRAADYIEG LDMLASMRLC ANVQAQYAIQ
     TALGGYQSIN DLIRPGGRLY EQRNIAWEML NEIPGVSCVK PEGAMYCFPR LDPNIYPIED
     DEKLMLDLLR AEKVLLVQGT GFNWPTPDHF RVVFLPAENE LREAIGRLGR FLANRR
//