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Database: UniProt
Entry: D4HYQ9_ERWAC
LinkDB: D4HYQ9_ERWAC
Original site: D4HYQ9_ERWAC 
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}.
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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
//
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