(data stored in ACNUC7421 zone)

HOGENOM: PROMH_1_PE1006

ID   PROMH_1_PE1006                       STANDARD;      PRT;   381 AA.
AC   PROMH_1_PE1006; B4ETL5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate
DE   aminotransferase; EC=2.6.1 87;AltName:
DE   Full=UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate)
DE   aminotransferase; Short=UDP-Ara4O aminotransferase;AltName:
DE   Full=UDP-4-amino-4-deoxy-L-arabinose aminotransferase; (PROMH_1.PE1006).
GN   Name=arnB; OrderedLocusNames=PMI1043;
OS   PROTEUS MIRABILIS HI4320.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROMH_1.PE1006.
CC       Proteus mirabilis HI4320 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:ARNB_PROMH
CC   -!- FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-
CC       Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The
CC       modified arabinose is attached to lipid A and is required for
CC       resistance to polymyxin and cationic antimicrobial peptides (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-4-amino-4-deoxy-beta-L-arabinose + 2-
CC       oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + glutamate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-
CC       beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
CC       arabinose from UDP-alpha-D-glucuronate: step 2/3.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the degT/dnrJ/eryC1 family. ArnB subfamily.
CC   -!- GENE_FAMILY: HOG000230163 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B4ETL5; -.
DR   EMBL; AM942759; CAR42269.1; -; Genomic_DNA.
DR   RefSeq; YP_002150793.1; NC_010554.1.
DR   ProteinModelPortal; B4ETL5; -.
DR   STRING; B4ETL5; -.
DR   GeneID; 6800148; -.
DR   GenomeReviews; AM942759_GR; PMI1043.
DR   OMA; NVTCAEG; -.
DR   ProtClustDB; PRK11658; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   HAMAP; MF_01167; ArnB_transfer; 1; -.
DR   InterPro; IPR022850; ArnB_NH2Trfase.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   HOGENOMDNA; PROMH_1.PE1006; -.
KW   Aminotransferase; Antibiotic resistance; Complete proteome;
KW   Lipid A biosynthesis; Lipid synthesis;
KW   Lipopolysaccharide biosynthesis; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   381 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSHFLPFSRP AIGDEEIKAV ESVLRSGWIT TGPQNHQLEQ DFCEKFGSKH AIAVCSATAG
     MHVVLMAMGI GPGDEVITPS QTWVSTINII TLLGAEPVMV DIDRDTLMVS AESVKKAITP
     RTKAIIPVHY AGAPCDLDAL RAVADEAGIP LIEDAAHAIG TRYKDEWIGE KGTSIFSFHA
     IKNVTCAEGG LVVTDDDELA NRVRCLKFHG LGVDAFDRQV QGRKPQAEVV EPGYKYNLSD
     IHAAIAVVQL SRLEEMNAKR AELVALYREK LQDSPLEMLS VPEYPHLHAN HLFMVRVDKN
     ACGIDRDTFM EKLKQKEIGT GLHFRAAHTQ KYYRERYPSL SLPQSEWNSA TLCSLPLFPD
     MSNKDVIRVV DAINEILSEH I
//

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