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
