ALAA_MYCBO
ID ALAA_MYCBO Reviewed; 429 AA.
AC P63499; A0A1R3XV17; O33267; X2BEM9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Alanine aminotransferase {ECO:0000250|UniProtKB:P9WQ91};
DE EC=2.6.1.2 {ECO:0000250|UniProtKB:P9WQ91};
DE AltName: Full=Alanine transaminase {ECO:0000250|UniProtKB:P9WQ91};
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=BQ2027_MB0344C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC Evidence={ECO:0000250|UniProtKB:P9WQ91};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q56232};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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; LT708304; SIT98893.1; -; Genomic_DNA.
DR RefSeq; NP_854008.1; NC_002945.3.
DR RefSeq; WP_003401733.1; NC_002945.4.
DR AlphaFoldDB; P63499; -.
DR SMR; P63499; -.
DR GeneID; 45424303; -.
DR PATRIC; fig|233413.5.peg.374; -.
DR OMA; WRMGWII; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004021; F:L-alanine: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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT CHAIN 1..429
FT /note="Alanine aminotransferase"
FT /id="PRO_0000123844"
FT BINDING 65
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P0A959"
FT BINDING 204
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P0A959"
FT BINDING 403
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P0A959"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
SQ SEQUENCE 429 AA; 47350 MW; 7B4944351190071A CRC64;
MDNDGTIVDV TTHQLPWHTA SHQRQRAFAQ SAKLQDVLYE IRGPVHQHAA RLEAEGHRIL
KLNIGNPAPF GFEAPDVIMR DIIQALPYAQ GYSDSQGILS ARRAVVTRYE LVPGFPRFDV
DDVYLGNGVS ELITMTLQAL LDNGDQVLIP SPDYPLWTAS TSLAGGTPVH YLCDETQGWQ
PDIADLESKI TERTKALVVI NPNNPTGAVY SCEILTQMVD LARKHQLLLL ADEIYDKILY
DDAKHISLAS IAPDMLCLTF NGLSKAYRVA GYRAGWLAIT GPKEHASSFI EGIGLLANMR
LCPNVPAQHA IQVALGGHQS IEDLVLPGGR LLEQRDIAWT KLNEIPGVSC VKPAGALYAF
PRLDPEVYDI DDDEQLVLDL LLSEKILVTQ GTGFNWPAPD HLRLVTLPWS RDLAAAIERL
GNFLVSYRQ
