ID Q57EK4_BRUAB Unreviewed; 367 AA.
AC Q57EK4;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Perosamine synthase, hypothetical {ECO:0000313|EMBL:AAX73930.1};
GN OrderedLocusNames=BruAb1_0544 {ECO:0000313|EMBL:AAX73930.1};
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698 {ECO:0000313|EMBL:AAX73930.1, ECO:0000313|Proteomes:UP000000540};
RN [1] {ECO:0000313|EMBL:AAX73930.1, ECO:0000313|Proteomes:UP000000540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941 {ECO:0000313|EMBL:AAX73930.1,
RC ECO:0000313|Proteomes:UP000000540};
RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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; AE017223; AAX73930.1; -; Genomic_DNA.
DR RefSeq; WP_002963679.1; NC_006932.1.
DR AlphaFoldDB; Q57EK4; -.
DR SMR; Q57EK4; -.
DR EnsemblBacteria; AAX73930; AAX73930; BruAb1_0544.
DR GeneID; 3787275; -.
DR KEGG; bmb:BruAb1_0544; -.
DR HOGENOM; CLU_033332_2_4_5; -.
DR Proteomes; UP000000540; Chromosome I.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 367 AA; 40498 MW; 5466D8623EB30918 CRC64;
MDIPVYSPYL CGNFKKYVNE CLDTGWISSR GEFISRFEDA FAQYVDVPSA ASVANGTVAL
HLALDALGIG AGDEVIVPTF TYIASVNTIL QTGATPVYVD SLENTLQIDP EGVRLAITER
TKAVMVVHLY GHPCDMDSIR EICDEKSLLL VEDCAEGFGT KWKNSHVGTF GDVATFSFFG
NKTITTGEGG MVLARNPQVM EKCRHLKSQG TSPTREYWHD ALAYNYRMTN IQAAIGLSQI
EMADEILSLK ARTAASYASK LAGLPLRMHT PVGDVKHSYW MCSIVLDNSE HREPLRQHLR
ENGVDTRPFF PPAHRMPHSA STGSYPVADS LSARGLNLPS FPHITDVEIS FVCDLVRSYF
SNHSNHI
//
