ID E5AQP5_MYCRK Unreviewed; 410 AA. AC E5AQP5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 56. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN OrderedLocusNames=RBRH_03675 {ECO:0000313|EMBL:CBW74927.1}; OS Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454) OS (Paraburkholderia rhizoxinica). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Mycetohabitans. OX NCBI_TaxID=882378 {ECO:0000313|EMBL:CBW74927.1, ECO:0000313|Proteomes:UP000007437}; RN [1] {ECO:0000313|EMBL:CBW74927.1, ECO:0000313|Proteomes:UP000007437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19002 / CIP 109453 / HKI 454 RC {ECO:0000313|Proteomes:UP000007437}; RX PubMed=21131495; DOI=10.1128/JB.01318-10; RA Lackner G., Moebius N., Partida-Martinez L., Hertweck C.; RT "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont of RT Rhizopus microsporus."; RL J. Bacteriol. 193:783-784(2011). 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; FR687359; CBW74927.1; -; Genomic_DNA. DR RefSeq; WP_013435156.1; NC_014722.1. DR AlphaFoldDB; E5AQP5; -. DR STRING; 882378.RBRH_03675; -. DR KEGG; brh:RBRH_03675; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_017584_4_2_4; -. DR OrthoDB; 9803354at2; -. DR Proteomes; UP000007437; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. 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:CBW74927.1}; KW Transferase {ECO:0000313|EMBL:CBW74927.1}. FT DOMAIN 37..388 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 410 AA; 45396 MW; 67F05077CC7A67C8 CRC64; MAVKPILKSH KLSNVCYDIR GPVLEEAKRL EEEGHRIIKL NIGNLAAFGF DAPDEIITDM IRNLPESSGY SDSKGVFAAR KSVMHYTQQK GIVDVKLDDI FIGNGASELI VMAMQGLLND GDEVLLPAPD YPLWTAAVSL SGGTPVHYRC DEYNGWLPDL DDMRAKISPN TRAMVIINPN NPTGALYPDD LVRAMLELAR QHQLIVFSDE VYDKIVYDGG VHTSVGALSQ DVLTVTFNSL SKSYRSCGYR AGWMVVSGDK RHATDYLEGL GILASMRLCA NVPGQYAIQT ALGGYQSIDE LIQPGGRLYK QRELAYDMLS AIPGVSVVKP KAALYMFPRL DPAVYPVRDD QQLILELLQQ ERVLLVQGTG FNWPAPDHFR VVFLPNVDDL GDSLSRVARF LDGYRKRTSA //