ARNA_PECCP
ID ARNA_PECCP Reviewed; 672 AA.
AC C6DAW5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=PC1_2926;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT13949.1; -; Genomic_DNA.
DR RefSeq; WP_015841105.1; NC_012917.1.
DR AlphaFoldDB; C6DAW5; -.
DR SMR; C6DAW5; -.
DR STRING; 561230.PC1_2926; -.
DR EnsemblBacteria; ACT13949; ACT13949; PC1_2926.
DR KEGG; pct:PC1_2926; -.
DR eggNOG; COG0223; Bacteria.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_23_1_6; -.
DR OMA; VRYCVKY; -.
DR OrthoDB; 2009156at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00492.
DR UniPathway; UPA00032; UER00494.
DR Proteomes; UP000002736; 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..672
FT /note="Bifunctional polymyxin resistance protein ArnA"
FT /id="PRO_1000213730"
FT REGION 1..310
FT /note="Formyltransferase ArnAFT"
FT REGION 320..672
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 440
FT /note="Proton acceptor; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT ACT_SITE 625
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 353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 374..375
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 399
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 404
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 438..439
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 466
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 498
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 532..541
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 619
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 672 AA; 75416 MW; 28BE7F5CBE4EB584 CRC64;
MKAIVFAYHD IGCVGLEALK LAGYEIQAVF THSDAPGENH FYASVAKAAA EMDVPVFAPE
DVNHPLWVNR IRELAPDVIF SFYYRTLLSD DILQLPSFGA FNLHGSLLPR YRGRAPVNWV
LVNGETQTGV TLHKMVSRAD AGDIVAQSVV EIDDEDTALT LHGKCRTTAA ALLAQQLPLI
RSREIMLTPQ DESQASYFGR RTAADGLIDW QKSAREINNL IRAVTEPYPG AFTFLGERKV
VIWRARVLKN DSVKANGVKQ EPGSIISTSP LVVSCGEDAL EIVSGQSESG LYMSGSRLAA
EMGMVPQAKL GNLASRVQRR RTRVLILGVN GFIGNHLTER LLRDDRYEIY GLDISSDAIA
RFLGDPRFHF VEGDISIHNE WIEYHIKKCD VILPLVAIAT PIEYTRNPLR VFELDFEENL
KIVRDCVRYN KRIVFPSTSE VYGMCDDKEF DEDTSRLIVG PINKQRWIYS VSKQLLDRVI
WAYGAKNGLR FTLFRPFNWM GPRLDTLDAA RIGSSRAITQ LILNLVEGSP IKLVDGGAQK
RCFTDIHDGI EALFRIIENR NGQCDGQIIN IGNPHNEASI RELGDMLLTS FNAHPLRDRF
PPFAGFIEVE SSSYYGKGYQ DVAHRTPSIR NAKRLLEWEP TVKMEQTVAE TLDYFLRTVD
PQHADNVTDT QG
