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}.
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; 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
//