ID Q45378_BORPT Unreviewed; 366 AA.
AC Q45378;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase {ECO:0000313|EMBL:SUV63430.1};
DE EC=2.6.1.87 {ECO:0000313|EMBL:SUV63430.1};
DE SubName: Full=WlbC protein {ECO:0000313|EMBL:CAA62247.1};
GN Name=wlbC {ECO:0000313|EMBL:CAA62247.1};
GN Synonyms=arnB_2 {ECO:0000313|EMBL:SUV63430.1};
GN ORFNames=NCTC10911_00431 {ECO:0000313|EMBL:SUV63430.1};
OS Bordetella pertussis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=520 {ECO:0000313|EMBL:CAA62247.1};
RN [1] {ECO:0000313|EMBL:CAA62247.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BP536 {ECO:0000313|EMBL:CAA62247.1};
RX PubMed=8821935; DOI=10.1046/j.1365-2958.1996.354877.x;
RA Allen A.G., Maskell D.J.;
RT "The identification, cloning and mutagenesis of a genetic locus required
RT for lipopolysaccharide biosynthesis in Bordetella pertussis.";
RL Mol. Microbiol. 19:37-52(1996).
RN [2] {ECO:0000313|EMBL:CAA62247.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BP536 {ECO:0000313|EMBL:CAA62247.1};
RA Reeves P.R., Hobbs M., Valvano M.A., Skurnik M., Whitfield C., Coplin D.,
RA Kido N., Klena J., Maskell D., Raetz C.R.H., Rick P.D.;
RT "Bacterial polysaccharide synthesis and gene nomenclature.";
RL Trends Microbiol. 49:495-503(1996).
RN [3] {ECO:0000313|EMBL:SUV63430.1, ECO:0000313|Proteomes:UP000255014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10911 {ECO:0000313|EMBL:SUV63430.1,
RC ECO:0000313|Proteomes:UP000255014};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {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; X90711; CAA62247.1; -; Genomic_DNA.
DR EMBL; UFTT01000002; SUV63430.1; -; Genomic_DNA.
DR PIR; S70674; S70674.
DR RefSeq; WP_010929614.1; NZ_UIGD01000005.1.
DR AlphaFoldDB; Q45378; -.
DR GeneID; 69603651; -.
DR PATRIC; fig|520.171.peg.93; -.
DR OMA; YGQCADF; -.
DR Proteomes; UP000255014; Unassembled WGS sequence.
DR GO; GO:0099620; F:UDP-4-amino-4-deoxy-L-arabinose aminotransferase; IEA:UniProtKB-EC.
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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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 Aminotransferase {ECO:0000313|EMBL:SUV63430.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:SUV63430.1}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 366 AA; 39505 MW; CBDA44FC3FB8FE18 CRC64;
MQFIDLKTQY QALRDTINPR IQAVLDHGQF IMGPEVKELE AALCAYTGAK HCITVASGTE
ALLISLMALG VKAGDEVITT SFTFVATAEV IALLGAKPVF VDVEPDTCNI KVSEIEAKIT
PRTKAIIPVS LYGQCGDMDE VNAVAARHGL PVIEDAAQSF GATYKGRKSC NLSTIGCTSF
FPSKPLGCYG DGGALFTNDD ELAQAMREIR VHGQSGRYYH ARIGVGGRMD TLQCAVVLGK
LERFDWEIAQ RIKIGARYQQ LLADLPGGAC TVTVRPDRDS VWAQFTVMVP NREAVIAQLK
EAGIPTAVHY PRPIHAQPAY EQYAEGAGAT PVSDDLAARV MSLPMHPDLD EATQDKIVAA
LRQALN
//
