ID D4GJ55_PANAM Unreviewed; 421 AA. AC D4GJ55; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAR-2024, entry version 52. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN Name=yfbQ {ECO:0000313|EMBL:ADD77805.1}; GN OrderedLocusNames=PANA_2638 {ECO:0000313|EMBL:ADD77805.1}; OS Pantoea ananatis (strain LMG 20103). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD77805.1, ECO:0000313|Proteomes:UP000001702}; RN [1] {ECO:0000313|EMBL:ADD77805.1, ECO:0000313|Proteomes:UP000001702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD77805.1, RC ECO:0000313|Proteomes:UP000001702}; RX PubMed=20348253; DOI=10.1128/JB.00060-10; RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F., RA Coutinho T.A.; RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of RT Eucalyptus blight and dieback."; RL J. Bacteriol. 192:2936-2937(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; CP001875; ADD77805.1; -; Genomic_DNA. DR AlphaFoldDB; D4GJ55; -. DR STRING; 706191.PANA_2638; -. DR KEGG; pam:PANA_2638; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_017584_4_2_6; -. DR Proteomes; UP000001702; Chromosome. 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 Reference proteome {ECO:0000313|Proteomes:UP000001702}. FT DOMAIN 51..404 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 421 AA; 47120 MW; 34C19E12AA015068 CRC64; MFSAAGTRIL HIKAATMTFQ IDKSGKLDNV CYDIRGPVLK EAKRLEEEGN KVLKLNIGNP APFGFEAPDE ILVDVIRNLP SAQGYCDSKG LYSARKAIMQ HYQARDMRDV TVEDIYIGNG VSELIVQAMQ ALLNSGDEML VPAPDYPLWT AAVSLSSGKA VHYLCDESAG WFPDLDDIRS KITPRTRGIV IINPNNPTGA VYSKALLMEV VEIARQHNLI IFADEIYDKI LYDDAQHHSI AALAPDLLTV TFNGLSKTYR VAGFRQGWMV LNGPKKHAKG YIEGLEMLAS MRLCANVPAQ HAIQTALGGY QSISEFIVPG GRLYEQRQRA WELINDIPGV SCVKPQGALY MFPRIDAKKF NIHDDQKMVL DFLLQEKVLL VQGTAFNWPW PDHLRIVTLP RVDDLEMAIN KFGRFLQGYR Q //