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ARNA_PSEA8
ID   ARNA_PSEA8              Reviewed;         662 AA.
AC   B7VBN2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=PLES_14791;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
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; FM209186; CAW26207.1; -; Genomic_DNA.
DR   RefSeq; WP_003119539.1; NC_011770.1.
DR   AlphaFoldDB; B7VBN2; -.
DR   SMR; B7VBN2; -.
DR   KEGG; pag:PLES_14791; -.
DR   HOGENOM; CLU_007383_23_0_6; -.
DR   OMA; VRYCVKY; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00492.
DR   UniPathway; UPA00032; UER00494.
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..662
FT                   /note="Bifunctional polymyxin resistance protein ArnA"
FT                   /id="PRO_1000137944"
FT   REGION          1..307
FT                   /note="Formyltransferase ArnAFT"
FT   REGION          316..662
FT                   /note="Dehydrogenase ArnADH"
FT   ACT_SITE        106
FT                   /note="Proton donor; for formyltransferase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   ACT_SITE        436
FT                   /note="Proton acceptor; for decarboxylase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   ACT_SITE        620
FT                   /note="Proton donor; for decarboxylase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         116
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         138..142
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         349
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         370..371
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         395
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         400
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         434..435
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         462
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         493
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         527..536
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   BINDING         614
FT                   /ligand="UDP-alpha-D-glucuronate"
FT                   /ligand_id="ChEBI:CHEBI:58052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   SITE            104
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT   SITE            142
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
SQ   SEQUENCE   662 AA;  74315 MW;  77ED67C25FE4E4D3 CRC64;
     MTSKAVVFAY HDIGCTGIEA LLNAGYEIAA VFTHADDPRE NTFYASVARL CAERGIPLHA
     PEDVNHPLWL ERIRQLRPDF LFSFYYRRLL GAELLACAAR GAYNLHGSLL PRYRGRAPAN
     WVLVNGETQT GVTLHRMIER ADAGPILAQQ AVAIDPEDTA LSLHGKLRKA AGALLRDSLP
     LLALGVLPEV EQDESQASHF GRRTPADGLL DWHRPARQLY DLVRAVTQPY PGAFCQVGEQ
     KLIVWSAEVV AGNHGREPGS VLSCDPLRIA CGEDSLVLRF GQRGERGLYL AGTQLATELG
     LVEGARLRGA ASGPQRRTRV LILGVNGFIG NHLSERLLRD GRYEVHGMDI GSDAIERLKA
     DPHFHFVEGD IGIHSEWLEY HVKKCDVILP LVAIATPIEY TRNPLRVFEL DFEENLRIVR
     YCVKYGKRVV FPSTSEVYGM CQDPDFDEDR SNLVVGPINK QRWIYSVSKQ LLDRVIWAYG
     QQGLRFTLFR PFNWMGPRLD RLDSARIGSS RAITQLILHL VEGTPIRLVD GGAQKRCFTD
     VDDGIEALAR IIDNRDGRCD GQIVNIGNPD NEASIRQLGE ELLRQFEAHP LRAQFPPFAG
     FREVESRSFY GDGYQDVAHR KPSIDNARRL LDWQPTIELR ETIGKTLDFF LHEALREREA
     QA
 
 
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