Y2045_ALKPO
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 03-AUG-2022, entry version 111.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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}.
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DR EMBL; L02548; 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 EnsemblBacteria; ADC50098; ADC50098; BpOF4_10225.
DR KEGG; bpf:BpOF4_10225; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_9; -.
DR OMA; HKIPSHY; -.
DR OrthoDB; 1322538at2; -.
DR Proteomes; UP000001544; 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 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