(data stored in ACNUC7421 zone)

HOGENOM: PROMH_1_PE1008

ID   PROMH_1_PE1008                       STANDARD;      PRT;   660 AA.
AC   PROMH_1_PE1008; B4ETL7;
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=Bifunctional polymyxin resistance protein ArnA;Includes:
DE   RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase;
DE   EC=2.1.2.13; AltName: Full=ArnAFT; AltName: Full=UDP-L-Ara4N
DE   formyltransferase;Includes: RecName: Full=UDP-glucuronic acid oxidase,
DE   UDP-4-keto-hexauronic acid decarboxylating; EC=1.1.1 305; AltName:
DE   Full=ArnADH; AltName: Full=UDP-GlcUA decarboxylase; AltName:
DE   Full=UDP-glucuronic acid dehydrogenase; (PROMH_1.PE1008).
GN   Name=arnA; OrderedLocusNames=PMI1045;
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.PE1008.
CC       Proteus mirabilis HI4320 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:ARNA_PROMH
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the oxidative
CC       decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-
CC       arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-
CC       amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-
CC       arabinose (UDP-L-Ara4FN). The modified arabinose is attached to
CC       lipid A and is required for resistance to polymyxin and cationic
CC       antimicrobial peptides (By similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-
CC       threo-pentapyranos-4-ulose + CO(2) + NADH.
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + UDP-4-amino-4-
CC       deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-
CC       formamido-beta-L-arabinose.
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 1/3.
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 3/3.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SUBUNIT: Homohexamer, formed by a dimer of trimers (By
CC       similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the fmt family.
CC       UDP-L-Ara4N formyltransferase subfamily.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the sugar
CC       epimerase family. UDP-glucuronic acid decarboxylase subfamily.
CC   -!- GENE_FAMILY: HOG000247761 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B4ETL7; -.
DR   EMBL; AM942759; CAR42271.1; -; Genomic_DNA.
DR   RefSeq; YP_002150795.1; NC_010554.1.
DR   ProteinModelPortal; B4ETL7; -.
DR   STRING; B4ETL7; -.
DR   GeneID; 6800077; -.
DR   GenomeReviews; AM942759_GR; PMI1045.
DR   OMA; KAVVFAY; -.
DR   ProtClustDB; PRK08125; -.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase 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_01166; ArnA; 1; -.
DR   InterPro; IPR021168; Bifun_polymyxin_resist_ArnA.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR011034; Formyl_transferase_C-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.10.25.10; Formyl_trans_C; 1.
DR   Gene3D; G3DSA:3.40.50.170; Formyl_transf_N; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PIRSF; PIRSF036506; Bifun_polymyxin_resist_ArnA; 1.
DR   SUPFAM; SSF50486; FMT_C_like; 1.
DR   SUPFAM; SSF53328; formyl_transf; 1.
DR   HOGENOMDNA; PROMH_1.PE1008; -.
KW   Antibiotic resistance; Complete proteome; Lipid A biosynthesis;
KW   Lipid synthesis; Lipopolysaccharide biosynthesis; Methyltransferase;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Transferase.
SQ   SEQUENCE   660 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKAIVFAYHD IGCVGLKALE KAGFDIQAVF THTDDPNENH FFSSVARVSA EMGLTVFAPE
     NVNHPLWIER IREMKPDVIF SFYYRHMLSD EILNLAPKGA FNLHGSLLPK YRGRAPINWA
     IVNGETETGV TLHKMTAKAD AGDIVAQEKV TIEDTDTSLI LHEKVREAAA KLMAHTLPHI
     ASGNYSTTAQ DESQATYYGR RCADDGLIDW NADAKTVHNL VRAVTEPYPG AFTFLGERKM
     IIWRARPVAD NQGKRPGTVI STEPLVIACA KGAIEVITGQ SENGLYVQGS RLATEMGIVT
     DVRVGPKATA QVKRRQRVLI LGVNGFIGNH LTERLLKDGN YDIYGMDIGS SAIERFIGNP
     RFHFIEGDVS IHTEWIEYHI KKCDVILPLV AIATPIEYTR NPLRVFELDF EENLKIVRYC
     VKYNKRIIFP STSEVYGMCD DKEFDEDNSR LIVGPINKQR WIYSVSKQLL DRVIWAYGAK
     EGLKFTLFRP FNWMGPRLDN LNSARIGSSR AITQLILNLV EGSPIKLVDG GEQKRCFTDI
     NDGIEALFRI IENRDNKCDG QIINIGNPTN EASIRELAEM LLDCFEKHEL RGHFPPFAGF
     KKIESSSYYG KGYQDVEHRK PSIKNAERLL DWKPTIETRQ TVEETLDFFL RGAVEELGNK
//

If you have problems or comments...

PBIL Back to PBIL home page