ID ARNB_PSEU2 Reviewed; 382 AA.
AC Q4ZSZ4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
DE EC=2.6.1.87 {ECO:0000255|HAMAP-Rule:MF_01167};
DE AltName: Full=Polymyxin resistance protein PmrH;
DE AltName: Full=UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
DE Short=UDP-Ara4O aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
DE AltName: Full=UDP-4-amino-4-deoxy-L-arabinose aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
GN Name=arnB {ECO:0000255|HAMAP-Rule:MF_01167}; OrderedLocusNames=Psyr_2689;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC -!- FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O)
CC to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified
CC arabinose is attached to lipid A and is required for resistance to
CC polymyxin and cationic antimicrobial peptides. {ECO:0000255|HAMAP-
CC Rule:MF_01167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + UDP-4-amino-4-deoxy-beta-L-arabinose = L-
CC glutamate + UDP-beta-L-threo-pentopyranos-4-ulose;
CC Xref=Rhea:RHEA:24710, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58708, ChEBI:CHEBI:58710; EC=2.6.1.87;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01167};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01167};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
CC arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from
CC UDP-alpha-D-glucuronate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01167}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01167}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01167}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01167}.
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DR EMBL; CP000075; AAY37728.1; -; Genomic_DNA.
DR RefSeq; WP_011267890.1; NC_007005.1.
DR RefSeq; YP_235766.1; NC_007005.1.
DR AlphaFoldDB; Q4ZSZ4; -.
DR SMR; Q4ZSZ4; -.
DR STRING; 205918.Psyr_2689; -.
DR KEGG; psb:Psyr_2689; -.
DR PATRIC; fig|205918.7.peg.2749; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_6; -.
DR OrthoDB; 9804264at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR Proteomes; UP000000426; Chromosome.
DR GO; GO:0099620; F:UDP-4-amino-4-deoxy-L-arabinose aminotransferase; IEA:UniProtKB-EC.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 HAMAP; MF_01167; ArnB_transfer; 1.
DR InterPro; IPR022850; ArnB_NH2Trfase.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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; Antibiotic resistance; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..382
FT /note="UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate
FT aminotransferase"
FT /id="PRO_0000110024"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ SEQUENCE 382 AA; 41810 MW; 132B1C58CB8E27A9 CRC64;
MSQTFLAFSR PSIGDEEIAA VTRVLRSGWI TTGPECQKLE EEFAARVGAR HAVALSSATG
AMHVALLALG VGPGDEVITP SQTWVSTANM ICLLGATPVF VDVDRDTLMT SAALIEHAIT
PRTKAIVPVH YAGAAFDLDP LYALADRHGI TVIEDAAHAA GTAYQGRPVG QQGTAIFSFH
AIKNMTCAEG AMLVTDNARL ADRVRQLKFH GLGVDAYDRL TLGRKPQAEV MEPGFKYNLA
DINASIARVQ LQRLDAINAQ RQALASHYLE RLANSPVLPL ALPRYAQQHA WHLFILRIDP
ERCGLDRDAF MKALQARNIG TGIHFIATHL HSYYRKRFPD VRLPDTEWNS SRLCSIPLFP
DMSLDDVERV VGAIESTLES SH
//
