ID Y2045_ALKPO Reviewed; 445 AA. AC P30268; D3FTM5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 2. DT 02-SEP-2026, entry version 122. DE RecName: Full=Uncharacterized aminotransferase BpOF4_10225; DE EC=2.6.-.-; DE AltName: Full=ORF B; GN OrderedLocusNames=BpOF4_10225; OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4) OS (Bacillus pseudofirmus). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Alkalihalophilus. OX NCBI_TaxID=398511; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Quirk P.G., Krulwich T.A.; RL Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4; RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x; RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J., RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B., RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y., RA Hu F.Z., Krulwich T.A.; RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that RT support the ability to grow in an external pH range from 7.5 to 11.4."; RL Environ. Microbiol. 13:3289-3309(2011). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000305}; CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. 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; AH000868; AAA22560.1; -; Genomic_DNA. DR EMBL; CP001878; ADC50098.1; -; Genomic_DNA. DR PIR; S27492; S27492. DR RefSeq; WP_012957464.1; NC_013791.2. DR AlphaFoldDB; P30268; -. DR SMR; P30268; -. DR STRING; 398511.BpOF4_10225; -. DR KEGG; bpf:BpOF4_10225; -. DR eggNOG; COG0160; Bacteria. DR HOGENOM; CLU_016922_10_0_9; -. DR Proteomes; UP000001544; Chromosome. DR GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-ARBA. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 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; IPR050103; Class-III_PLP-dep_AT. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; NF005993; PRK08117.1; 1. DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..445 FT /note="Uncharacterized aminotransferase BpOF4_10225" FT /id="PRO_0000120537" FT MOD_RES 280 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255" FT CONFLICT 296 FT /note="K -> T (in Ref. 1; AAA22560)" FT /evidence="ECO:0000305" SQ SEQUENCE 445 AA; 48876 MW; 0D7D11874DC9B995 CRC64; MSADWSYLRE KSASRLAPSM AKDHPNLPVV KEEGCYYYGV DGVKYLDFTS GIAVTNVGHR HPKIVQAIKE AADHLTHGPI GVIQYESILK LADELADILP GDLDCFFFAN SGTEAIEGAL KLAKFVTKRP YVVSFTGCFH GRTQGSLGVS TSKSKYRKFL QPNGLTYQVP YFKPSDPRIL DEEGEVVESL ACELLEEEFT NLFKYHVSSE EVAAVILEPV LGEGGYIIPP ASWLAKVREI CNRHDILLIF DEVQTGFGRT GEWFAAQTFG VTPDIMAIAK GIASGLPLSA TVANHKLMQQ WPLGSHGTTF GGNPIACSAA LATLDVLKEE NLLDNAREVG AYARERLNLL KEKYEMIGSI RSVGLMIGIE IIDPQTKKPD GAAVLRILDL ALQEGVLFYL CGNEGEVIRM IPPLSVTKEQ IDDGLDMLQR ALVKYKEETH QPASL //