ID D4HYQ9_ERWAC Unreviewed; 379 AA.
AC D4HYQ9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase {ECO:0000256|HAMAP-Rule:MF_01167};
DE EC=2.6.1.87 {ECO:0000256|HAMAP-Rule:MF_01167};
DE AltName: Full=UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase {ECO:0000256|HAMAP-Rule:MF_01167};
DE Short=UDP-Ara4O aminotransferase {ECO:0000256|HAMAP-Rule:MF_01167};
DE AltName: Full=UDP-4-amino-4-deoxy-L-arabinose aminotransferase {ECO:0000256|HAMAP-Rule:MF_01167};
GN Name=yfbE {ECO:0000313|EMBL:CBA20034.1};
GN Synonyms=arnB {ECO:0000256|HAMAP-Rule:MF_01167};
GN OrderedLocusNames=EAMY_1084 {ECO:0000313|EMBL:CBA20034.1};
OS Erwinia amylovora (strain CFBP1430).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA20034.1, ECO:0000313|Proteomes:UP000001841};
RN [1] {ECO:0000313|EMBL:CBA20034.1, ECO:0000313|Proteomes:UP000001841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841};
RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA Duffy B.;
RT "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT CFBP 1430 and comparison to other Erwinia spp.";
RL Mol. Plant Microbe Interact. 23:384-393(2010).
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:0000256|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:0000256|HAMAP-Rule:MF_01167};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01167};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01167}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01167}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01167}.
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; FN434113; CBA20034.1; -; Genomic_DNA.
DR RefSeq; WP_004156580.1; NC_013961.1.
DR AlphaFoldDB; D4HYQ9; -.
DR STRING; 665029.EAMY_1084; -.
DR GeneID; 8911461; -.
DR KEGG; eam:EAMY_1084; -.
DR PATRIC; fig|665029.3.peg.1065; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_6; -.
DR OMA; IVNHGMY; -.
DR OrthoDB; 9804264at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR Proteomes; UP000001841; 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: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; TRANSAMINASE; 1.
DR PANTHER; PTHR30244:SF41; UDP-4-AMINO-4-DEOXY-L-ARABINOSE--OXOGLUTARATE AMINOTRANSFERASE; 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:0000256|HAMAP-Rule:MF_01167,
KW ECO:0000313|EMBL:CBA20034.1};
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW Rule:MF_01167};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_01167};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01167};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01167};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW ECO:0000256|HAMAP-Rule:MF_01167};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01167,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01167, ECO:0000313|EMBL:CBA20034.1}.
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|HAMAP-Rule:MF_01167,
FT ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 379 AA; 41555 MW; CB32A90B45425D94 CRC64;
MSEFLPFSRP SMGAEELAAV EEVLRSGWIT TGPKNQQLEQ AFCQLTGNRH AIAVSSATAG
MHVVLMALGI GPGDEVITPS LTWVSTLNMI VLLGATPVMI DVDRDTLMVT PQLVEAAITA
RTRAIIPVHY AGAPADIEAI HALGKRHGIT VIDDAAHAAG TYYRGRHVGD SGTAIFSFHA
IKNISCAEGG MVVTDDDALA DRVRSLKFHG LGVDAFDRQT HGRAPQAEVL TPGFKYNLAD
INAAMAMAQL DKLAAHNARR EQIAQRYLDE LTDTPFLPLA RPVWPHRHAW HLFILRVDRE
SCGLSRDELM QQLKEQGIGS GLHFRAVHTQ KYYRERFPQL SLPETEWNSD RICSIPLFPG
MNDGDCDRVI AALRKLADG
//