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ARNA_KLEP3
ID   ARNA_KLEP3              Reviewed;         661 AA.
AC   B5XTK9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Bifunctional polymyxin resistance protein ArnA {ECO:0000255|HAMAP-Rule:MF_01166};
DE   Includes:
DE     RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase {ECO:0000255|HAMAP-Rule:MF_01166};
DE              EC=2.1.2.13 {ECO:0000255|HAMAP-Rule:MF_01166};
DE     AltName: Full=ArnAFT {ECO:0000255|HAMAP-Rule:MF_01166};
DE     AltName: Full=UDP-L-Ara4N formyltransferase {ECO:0000255|HAMAP-Rule:MF_01166};
DE   Includes:
DE     RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating {ECO:0000255|HAMAP-Rule:MF_01166};
DE              EC=1.1.1.305 {ECO:0000255|HAMAP-Rule:MF_01166};
DE     AltName: Full=ArnADH {ECO:0000255|HAMAP-Rule:MF_01166};
DE     AltName: Full=UDP-GlcUA decarboxylase {ECO:0000255|HAMAP-Rule:MF_01166};
DE     AltName: Full=UDP-glucuronic acid dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01166};
GN   Name=arnA {ECO:0000255|HAMAP-Rule:MF_01166}; OrderedLocusNames=KPK_0268;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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 lipid A
CC       and is required for resistance to polymyxin and cationic antimicrobial
CC       peptides. {ECO:0000255|HAMAP-Rule:MF_01166}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-
CC         threo-pentopyranos-4-ulose; Xref=Rhea:RHEA:24702, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58710; EC=1.1.1.305; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01166};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-
CC         arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-
CC         formamido-beta-L-arabinose; Xref=Rhea:RHEA:24706, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:58708,
CC         ChEBI:CHEBI:58709; EC=2.1.2.13; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01166};
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 1/3. {ECO:0000255|HAMAP-Rule:MF_01166}.
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 3/3. {ECO:0000255|HAMAP-Rule:MF_01166}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01166}.
CC   -!- SUBUNIT: Homohexamer, formed by a dimer of trimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01166}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the Fmt family. UDP-
CC       L-Ara4N formyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01166}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD(P)-dependent
CC       epimerase/dehydratase family. UDP-glucuronic acid decarboxylase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01166}.
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DR   EMBL; CP000964; ACI10935.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XTK9; -.
DR   SMR; B5XTK9; -.
DR   EnsemblBacteria; ACI10935; ACI10935; KPK_0268.
DR   KEGG; kpe:KPK_0268; -.
DR   HOGENOM; CLU_007383_23_2_6; -.
DR   OMA; VRYCVKY; -.
DR   OrthoDB; 2009156at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00492.
DR   UniPathway; UPA00032; UER00494.
DR   Proteomes; UP000001734; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0099619; F:UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0099618; F:UDP-glucuronic acid dehydrogenase activity; 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; cd05257; Arna_like_SDR_e; 1.
DR   HAMAP; MF_01166; ArnA; 1.
DR   InterPro; IPR045869; Arna-like_SDR_e.
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; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; SSF50486; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW   NAD; Oxidoreductase; Transferase.
FT   CHAIN           1..661
FT                   /note="Bifunctional polymyxin resistance protein ArnA"
FT                   /id="PRO_1000137943"
FT   REGION          1..304
FT                   /note="Formyltransferase ArnAFT"
FT   REGION          314..661
FT                   /note="Dehydrogenase ArnADH"
FT   ACT_SITE        104
FT                   /note="Proton donor; for formyltransferase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   ACT_SITE        434
FT                   /note="Proton acceptor; for decarboxylase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   ACT_SITE        619
FT                   /note="Proton donor; for decarboxylase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         114
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         136..140
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         347
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         368..369
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         393
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         398
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         432..433
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         460
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         492
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         526..535
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         613
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   SITE            102
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   SITE            140
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
SQ   SEQUENCE   661 AA;  74234 MW;  91F638D889E51855 CRC64;
     MKAVVFAYHD MGCTGIQSLL DAGYDIAAIF THPDNPGENH FFGSVARLAA EQGIPVWAPE
     DVNHPLWIER IREMKPDVLF SFYYRNLLGD EILNLAPKGA FNLHGSLLPK YRGRAPLNWV
     LVNGESETGV TLHRMVNRAD AGDIVAQQTV AIGPDDAALT LHRKLCAAAT ELLGQALPAI
     LEGKTAERPQ DHSQATYVGR RTPEDGRLDW EQPAQTLHNL VRAVSDPWPG AFGYAGANKF
     IVWKSRVRHD LPAAKPGTVI SVAPLIVACQ DGALEIVTGQ TERGVYMQGA QLAQALGLVS
     GAVISSKPVV AIKRRTRVLI LGVNGFIGNH LTERLLQDDN YEIYGLDIGS DAISRFLESP
     RFHFVEGDIS IHSEWIEYHI KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLKIIRDC
     VKYNKRIIFP STSEVYGMCT DKNFDEDTSN LVVGPINKQR WIYSVSKQLL DRVIWAYGDK
     YDLKFTLFRP FNWMGPRLDN LNAARIGSSR AITQLILNLV EGSPIKLIEG GKQKRCFTDI
     SDGIEALFRI IENKDGRCDG QIINIGNPEN EASIKELAEM LLACFERHPL RDRFPPFAGF
     REVESSDYYG KGYQDVEHRK PSIRNAKRCL NWEPKVEMEE TVEHTLDFFL RTVELVDDKN
     P
 
 
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