ID W1IKU2_9GAMM Unreviewed; 381 AA.
AC W1IKU2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=pgbP {ECO:0000313|EMBL:CDL79137.1};
GN Synonyms=arnB {ECO:0000256|HAMAP-Rule:MF_01167};
GN ORFNames=XCR1_1050017 {ECO:0000313|EMBL:CDL79137.1};
OS Xenorhabdus cabanillasii JM26.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL79137.1, ECO:0000313|Proteomes:UP000019197};
RN [1] {ECO:0000313|EMBL:CDL79137.1, ECO:0000313|Proteomes:UP000019197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM26 {ECO:0000313|EMBL:CDL79137.1,
RC ECO:0000313|Proteomes:UP000019197};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT Xenorhabdus cabanillasi strain JM26.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL79137.1}.
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DR EMBL; CBXE010000008; CDL79137.1; -; Genomic_DNA.
DR RefSeq; WP_038259540.1; NZ_NJGH01000038.1.
DR AlphaFoldDB; W1IKU2; -.
DR OrthoDB; 9804264at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR Proteomes; UP000019197; Unassembled WGS sequence.
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:CDL79137.1};
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:CDL79137.1}.
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 381 AA; 42516 MW; B2577EA60E0D18BA CRC64;
MDNFLPFSRP SIGNEEIKAV EKVLRSGWIT TGPQNQQLEQ DFARMFGCRH AIALYSATAG
MHLALLALGI GSGDEVITPS QTWVSTINMI CLLGAEPVMV DVDRDTLMVN AKTIKQAITP
KTKAIIPVHY AGAPCDLDAL RAVAKEADIP LIEDAAHAVG TRYKNEWVGE RGTAIFSFHA
IKNMTCAEGG MLVTDNDELA QRVRCLKFHG LAVDAFDRQI QGRKPQAEVI EPGFKYNLSD
IHAAVAVVQL SKLASMNARR RELVARYSSA LKDTPLQMLS VPEYEHWHSH HLFMVRVDQS
ICGIDRDTFM TRLKERNIGT GLHFRAVHTQ QYYRQRYPVL SLPESEWNSA TLCSLPLFPD
MNNDDADRVV NAVLEILAEC R
//
