ALAA_MYCTU
ID ALAA_MYCTU Reviewed; 429 AA.
AC P9WQ91; L0T6D2; O33267; P63498;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Alanine aminotransferase {ECO:0000305};
DE EC=2.6.1.2 {ECO:0000269|PubMed:32327655};
DE AltName: Full=Alanine transaminase {ECO:0000303|PubMed:32327655};
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=Rv0337c; ORFNames=MTCY279.04c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP CATALYTIC ACTIVITY.
RC STRAIN=H37Rv;
RX PubMed=32327655; DOI=10.1038/s41467-020-15876-8;
RA Jansen R.S., Mandyoli L., Hughes R., Wakabayashi S., Pinkham J.T.,
RA Selbach B., Guinn K.M., Rubin E.J., Sacchettini J.C., Rhee K.Y.;
RT "Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen
RT metabolism in Mycobacterium tuberculosis.";
RL Nat. Commun. 11:1960-1960(2020).
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:0000269|PubMed:32327655};
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}.
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DR EMBL; AL123456; CCP43067.1; -; Genomic_DNA.
DR PIR; H70506; H70506.
DR RefSeq; NP_214851.1; NC_000962.3.
DR RefSeq; WP_003401733.1; NZ_NVQJ01000081.1.
DR AlphaFoldDB; P9WQ91; -.
DR SMR; P9WQ91; -.
DR STRING; 83332.Rv0337c; -.
DR PaxDb; P9WQ91; -.
DR DNASU; 886522; -.
DR GeneID; 45424303; -.
DR GeneID; 886522; -.
DR KEGG; mtu:Rv0337c; -.
DR TubercuList; Rv0337c; -.
DR eggNOG; COG0436; Bacteria.
DR OMA; WRMGWII; -.
DR PhylomeDB; P9WQ91; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..429
FT /note="Alanine aminotransferase"
FT /id="PRO_0000123843"
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
