ID I7G268_MYCS2 Unreviewed; 430 AA.
AC I7G268;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN Name=aspC {ECO:0000313|EMBL:AFP37151.1};
GN OrderedLocusNames=MSMEI_0671 {ECO:0000313|EMBL:AFP37151.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:AFP37151.1, ECO:0000313|Proteomes:UP000006158};
RN [1] {ECO:0000313|EMBL:AFP37151.1, ECO:0000313|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000006158};
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [2] {ECO:0000313|EMBL:AFP37151.1, ECO:0000313|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000006158};
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP001663; AFP37151.1; -; Genomic_DNA.
DR AlphaFoldDB; I7G268; -.
DR KEGG; msg:MSMEI_0671; -.
DR PATRIC; fig|246196.56.peg.686; -.
DR Proteomes; UP000006158; 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:AFP37151.1};
KW Transferase {ECO:0000313|EMBL:AFP37151.1}.
FT DOMAIN 60..407
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47868 MW; 609C5CD5FA0A7697 CRC64;
MDSDETMERV TTHQLPWQST GEHRKPRTFT QSTKLQDVLY EIRGPVHEHA SRLEAEGHRI
LKLNIGNPAP FGFEAPDVIM RDIIQALPTA QGYSDSKGIL SARRAVFTRY ELVEGFPKFD
VDDVYLGNGV SELITMTLQA LLDNGDQVLI PAPDYPLWTA STSLAGGTPV HYLCDETQGW
NPDVADIESK ITERTKAIVV INPNNPTGAV YSRETLEQIV DLARKHQLLL LADEIYDKIL
YDDAKHISLA TLAPDLLCLT FNGLSKAYRV AGYRSGWLVI TGPKEHATSF IEGISLLANM
RLCPNVPAQH AIQVALGGHQ SIDALVLPGG RLLEQRDVAW EKLNEIPGVS CVKPRGALYA
FPRLDPEVYD IHDDEQLVLD LLLQEKILLT QGTGFNWPTP DHLRIVTLPW ARDLASAIER
LGNFLASYRQ
//