ID ARNA_SHIB3 Reviewed; 526 AA. AC B2TW38; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 87. DE RecName: Full=Putative bifunctional polymyxin resistance protein ArnA; DE Includes: DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase; DE EC=2.1.2.13; DE AltName: Full=ArnAFT; DE AltName: Full=UDP-L-Ara4N formyltransferase; DE Includes: DE RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating; DE EC=1.1.1.305; DE AltName: Full=ArnADH; DE AltName: Full=UDP-GlcUA decarboxylase; DE AltName: Full=UDP-glucuronic acid dehydrogenase; GN Name=arnA; OrderedLocusNames=SbBS512_E2631; OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=344609; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 3083-94 / BS512; RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R., RA Jiang L., Ravel J., Sebastian Y.; RT "Complete sequence of Shigella boydii serotype 18 strain BS512."; RL Submitted (MAY-2008) 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 (By similarity). {ECO:0000250}. 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; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-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:58708, ChEBI:CHEBI:58709, CC ChEBI:CHEBI:195366; EC=2.1.2.13; 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. 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. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. CC -!- SUBUNIT: Homohexamer, formed by a dimer of trimers. {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the Fmt family. UDP- CC L-Ara4N formyltransferase subfamily. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD(P)-dependent CC epimerase/dehydratase family. UDP-glucuronic acid decarboxylase CC subfamily. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. The N-terminal region is CC truncated when compared to orthologs. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001063; ACD07332.1; -; Genomic_DNA. DR AlphaFoldDB; B2TW38; -. DR SMR; B2TW38; -. DR STRING; 344609.SbBS512_E2631; -. DR KEGG; sbc:SbBS512_E2631; -. DR HOGENOM; CLU_007383_23_2_6; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00032; UER00492. DR UniPathway; UPA00032; UER00494. DR Proteomes; UP000001030; 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; cd08702; Arna_FMT_C; 1. DR CDD; cd05257; Arna_like_SDR_e; 1. DR Gene3D; 3.40.50.12230; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR045869; Arna-like_SDR_e. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR036477; Formyl_transf_N_sf. DR InterPro; IPR011034; Formyl_transferase-like_C_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1. DR PANTHER; PTHR43245:SF13; NAD(P)-BD_DOM DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01370; Epimerase; 1. DR Pfam; PF02911; Formyl_trans_C; 1. DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1. DR SUPFAM; SSF53328; Formyltransferase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 5: Uncertain; KW Antibiotic resistance; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Lipopolysaccharide biosynthesis; Multifunctional enzyme; KW NAD; Oxidoreductase; Reference proteome; Transferase. FT CHAIN 1..526 FT /note="Putative bifunctional polymyxin resistance protein FT ArnA" FT /id="PRO_0000379991" FT REGION 1..170 FT /note="Formyltransferase ArnAFT" FT REGION 180..526 FT /note="Dehydrogenase ArnADH" FT ACT_SITE 300 FT /note="Proton acceptor; for decarboxylase activity" FT /evidence="ECO:0000250" FT ACT_SITE 485 FT /note="Proton donor; for decarboxylase activity" FT /evidence="ECO:0000250" FT BINDING 2..6 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250" FT BINDING 213 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 234..235 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 259 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000250" FT BINDING 264 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000250" FT BINDING 298..299 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000250" FT BINDING 326 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000250" FT BINDING 358 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000250" FT BINDING 392..401 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000250" FT BINDING 479 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000250" FT SITE 6 FT /note="Raises pKa of active site His" FT /evidence="ECO:0000250" SQ SEQUENCE 526 AA; 59435 MW; AF2E061948764B2A CRC64; MVKRADAGAI VAQLRVAIAP DDIAITLHHK LCHAARQLLE QTLPAIKHGN ILEIAQRENE ATCFGRRTPD DSFLEWHKPA SVLHNMVRAV ADPWPSAFSY VGNQKFTVWS SRVHPHASKA QPGSVISIAP LLIACGDGAL EIVTGQAGDG ITMQGSQLAQ TLGLVQGSRL NSQPACTARR RTRVLILGVN GFIGNHLTER LLREDHYEVY GLDIGSDAIS RFLNHPHFHF VEGDISIHSE WIEYHVKKCD VVLPLVAIAT PIEYTRNPLR VFELDFEENL RIIRYCVKYR KRIIFPSTSE VYGMCSDKYF DEDHSNLIVG PVNKPRWIYS VSKQLLDRVI WAYGEKEGLQ FTLFRPFNWM GPRLDNLNAA RIGSSRAITQ LILNLVEGSP IKLIDGGKQK RCFTDIRDGI EALYRIIENA GNRCDGEIIN IGNPENEASI EELGKMLLAS FEKHPLRHHF PPFAGFRVVE SSSYYGKGYQ DVEHRKPSIR NAHRCLDWEP KIDMQETIDE TLDFFLRTVD LTDKPS //