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Database: UniProt
Entry: Q1LLY0_CUPMC
LinkDB: Q1LLY0_CUPMC
Original site: Q1LLY0_CUPMC 
ID   Q1LLY0_CUPMC            Unreviewed;       453 AA.
AC   Q1LLY0;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=aatA {ECO:0000313|EMBL:ABF08846.1};
GN   OrderedLocusNames=Rmet_1967 {ECO:0000313|EMBL:ABF08846.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF08846.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF08846.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1LLY0; -.
DR   STRING; 266264.Rmet_1967; -.
DR   KEGG; rme:Rmet_1967; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_4; -.
DR   OMA; CALDLCI; -.
DR   Proteomes; UP000002429; 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:ABF08846.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW   Transferase {ECO:0000313|EMBL:ABF08846.1}.
FT   DOMAIN          78..438
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   453 AA;  50377 MW;  C3799501E0D1C2A3 CRC64;
     MPPGLPRLAS LIADAPPDAQ DNPEIPRFRC RQRPAACPDI ANTAVKPIQK SHKLQNVCYD
     IRGPVLEKAK QMEEEGHKII KLNIGNLAVF GFDAPEEIQQ DMMRNLPNSA GYSDSKGIFA
     ARKAIMHYTQ EKKIQGVGLD DIYVGNGASE LIVMAMNALL NSGDEMLVPA PDYPLWTAAV
     SLSGGTPVHY VCDEANEWMP DLDDIRRKIT PNTRGIVIIN PNNPTGALYS DELLKEIVAI
     AREHGLIIFA DEIYDKVLYD GNTHTSIGSL STDVLTVTFN GLSKNYRSCG YRAGWMVVSG
     DKRPALDYIE GLNMLSSMRL CANVPGQWAI QTALGGYQSI NDLVTEGGRL RRQRDLAYEL
     ITKIPGVTCV KPKAALYLFP KLDLSMYPIQ DDQEFIYELL QESKVLLVQG TGFNWGAPDH
     FRIVFLPHEE DLREAITRVG RFLESYRKRH GTA
//
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