ID   A6SXK4_JANMA            Unreviewed;       407 AA.
AC   A6SXK4;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=aspB1 {ECO:0000313|EMBL:ABR88575.1};
GN   OrderedLocusNames=mma_1311 {ECO:0000313|EMBL:ABR88575.1};
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88575.1, ECO:0000313|Proteomes:UP000006388};
RN   [1] {ECO:0000313|EMBL:ABR88575.1, ECO:0000313|Proteomes:UP000006388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille {ECO:0000313|EMBL:ABR88575.1,
RC   ECO:0000313|Proteomes:UP000006388};
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88575.1; -; Genomic_DNA.
DR   RefSeq; WP_012079168.1; NC_009659.1.
DR   AlphaFoldDB; A6SXK4; -.
DR   STRING; 375286.mma_1311; -.
DR   KEGG; mms:mma_1311; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_4; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000006388; 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:ABR88575.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006388};
KW   Transferase {ECO:0000313|EMBL:ABR88575.1}.
FT   DOMAIN          34..395
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   407 AA;  45288 MW;  9ACA51887550A7F7 CRC64;
     MRPIQKSKKL DDVCYDIRGP VLEKARQMEE DGHKIIKLNI GNLAVFGFDA PDEIVQDMIR
     NMSNASGYTD SKGLFAPRKA IMHYTQEKKI TGVTIDDIYL GNGASELIVM SMNALLNTGD
     EVLVPSPDYP LWTAAVSLSG GKPVHYVCDE QADWFPDIED IKSKINSNTK AIVVINPNNP
     TGALYPVELL EQIVEVARQH QLIVFADEIY DKVLYDGNTH TSLASLADDV LFITFNGLSK
     NYRSCGYRAG WMVVSGEKRH ARDYIEGLNM LASMRLCANV PGQYAIQTAL GGYQSINDLV
     APGGRLLRQR DLAHKLLTEI PGVTCVKPKS ALYMFPRLDP KMYPIKDDQD FAQQLLVEES
     VLIVQGTGFN CPTTDHFRVV FLPNSDDLTV AVGRIAHFLE GYRKRLG
//