ID   A0A0D6EW77_9PROT        Unreviewed;       408 AA.
AC   A0A0D6EW77;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=yfbQ {ECO:0000313|EMBL:CEZ19528.1};
GN   ORFNames=BN1208_0642 {ECO:0000313|EMBL:CEZ19528.1};
OS   Candidatus Methylopumilus planktonicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylopumilus.
OX   NCBI_TaxID=1581557 {ECO:0000313|EMBL:CEZ19528.1, ECO:0000313|Proteomes:UP000064007};
RN   [1] {ECO:0000313|Proteomes:UP000064007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000064007};
RA   Salcher M.M.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LN827929; CEZ19528.1; -; Genomic_DNA.
DR   RefSeq; WP_046487825.1; NZ_LN827929.1.
DR   AlphaFoldDB; A0A0D6EW77; -.
DR   STRING; 1581557.BN1208_0642; -.
DR   KEGG; mbat:BN1208_0642; -.
DR   HOGENOM; CLU_017584_4_2_4; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000064007; Chromosome 1.
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:CEZ19528.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064007};
KW   Transferase {ECO:0000313|EMBL:CEZ19528.1}.
FT   DOMAIN          35..395
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   408 AA;  45685 MW;  35CB069C6332268D CRC64;
     MAQLKKSSKL NNVCYDIRGP VLAHAKKMEE EGQRIIKLNI GNPAAFGFEA PEEIVQDVIR
     NMGKASGYTD SKGLFEPRKS IMHYTQEKNI PNVDIDDVII GNGVSELIVM SMQALLDNDD
     EVLIPMPDYP LWNAAVTLAG GKPRHYLCDE ASNWYPDLKD IESKITSKTK AILVINPNNP
     TGALYPKEIL EGVIQIARKH KLVVFADEIY DKVIYDKKKH ISIGSLADDI LFVTLNGLSK
     NYRACGYRAG WLVVSGNKKE SADYIEGLNM LASMRLCANV PGQLAIQTAL GGYQSIDDLV
     APSGRLFKQR ELAYDMLVSI PGVTCVKPEA AMYLFPKLDP KIYPIKDDQE FILKLLIDKK
     VLLVQGTGFN WKDPDHIRIV FLPNEEDLKE SINRIADYLE NFKKNTAH
//