ID Q6AEY3_LEIXX Unreviewed; 445 AA. AC Q6AEY3; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 27-MAR-2024, entry version 92. DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AAT89062.1}; GN Name=gabT {ECO:0000313|EMBL:AAT89062.1}; GN OrderedLocusNames=Lxx12170 {ECO:0000313|EMBL:AAT89062.1}; OS Leifsonia xyli subsp. xyli (strain CTCB07). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Leifsonia. OX NCBI_TaxID=281090 {ECO:0000313|EMBL:AAT89062.1, ECO:0000313|Proteomes:UP000001306}; RN [1] {ECO:0000313|EMBL:AAT89062.1, ECO:0000313|Proteomes:UP000001306} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CTCB07 {ECO:0000313|EMBL:AAT89062.1, RC ECO:0000313|Proteomes:UP000001306}; RX PubMed=15305603; RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P., RA Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D., RA de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R., RA Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L., RA El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.; RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli RT subsp. xyli."; RL Mol. Plant Microbe Interact. 17:827-836(2004). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}. 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; AE016822; AAT89062.1; -; Genomic_DNA. DR AlphaFoldDB; Q6AEY3; -. DR STRING; 281090.Lxx12170; -. DR KEGG; lxx:Lxx12170; -. DR eggNOG; COG0160; Bacteria. DR HOGENOM; CLU_016922_10_0_11; -. DR Proteomes; UP000001306; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1. DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000313|EMBL:AAT89062.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; KW Reference proteome {ECO:0000313|Proteomes:UP000001306}; KW Transferase {ECO:0000313|EMBL:AAT89062.1}. SQ SEQUENCE 445 AA; 47320 MW; 584F9605D4B6AF40 CRC64; MTREFSVPQS RRIVTELPGP RSVELQRRRE ASVSRGAGTL ANIYMESGSG AILVDVDGNR LIDLGCGIGV TTIGHAHPAV AAAAAEQAAK LTHTLFTVTP YENYVRVAEK LAEITPGDVE KRSILVNSGA EAVENAVKIA RKHTGRRAIA TLDHAFHGRT NLTMAMTYRP WPERAGMGPF PGEIYSLPLS YPFRDPEGMI GEEAAERAID YINTHIGATE LAALFVEPIQ GDGGIVIPAP GYFKRLSEFC SENGIVFVAD EIQAGIGRTG TWYAIEHHGV VPDLITTAKG IAGGFPLAAV TGRAEIMDAV QPGGIGGTFG GNPVSTAAAL AVFEVVEREN LLDEAKRVER ALWARIGDWA ERFPVVGEVR GKGAMFGIEL VVPGTKKPNP EALRAVLAHA TGNGVIPLDA GSWDSVLRLL PSVVISEELI DDAATVIEAA LERLG //