ARNA_SHIB3
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 03-AUG-2022, entry version 81.
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; Proteobacteria; 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=(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;
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}.
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DR EMBL; CP001063; ACD07332.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TW38; -.
DR SMR; B2TW38; -.
DR STRING; 344609.SbBS512_E2631; -.
DR EnsemblBacteria; ACD07332; ACD07332; SbBS512_E2631.
DR KEGG; sbc:SbBS512_E2631; -.
DR HOGENOM; CLU_007383_23_2_6; -.
DR OMA; VRYCVKY; -.
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; cd05257; Arna_like_SDR_e; 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 Pfam; PF01370; Epimerase; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
PE 5: Uncertain;
KW Antibiotic resistance; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW NAD; Oxidoreductase; 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="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
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
