ARNA_ECOLC
ID ARNA_ECOLC Reviewed; 660 AA.
AC B1IXT2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=EcolC_1394;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-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. {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; CP000946; ACA77058.1; -; Genomic_DNA.
DR RefSeq; WP_000860273.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IXT2; -.
DR SMR; B1IXT2; -.
DR KEGG; ecl:EcolC_1394; -.
DR HOGENOM; CLU_007383_23_1_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..660
FT /note="Bifunctional polymyxin resistance protein ArnA"
FT /id="PRO_1000085380"
FT REGION 1..304
FT /note="Formyltransferase ArnAFT"
FT REGION 314..660
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 434
FT /note="Proton acceptor; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT ACT_SITE 619
FT /note="Proton donor; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 86..88
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
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 347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 368..369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 393
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 398
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 432..433
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 460
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 492
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 526..535
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 613
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 660 AA; 74289 MW; A430928AB4041FA3 CRC64;
MKTVVFAYHD MGCLGIEALL AAGYEISAIF THTDNPGEKA FYGSVARLAA ERGIPVYAPD
NVNHPLWVER IAQLSPDVIF SFYYRHLIYD EILQLAPAGA FNLHGSLLPK YRGRAPLNWV
LVNGETETGV TLHRMVKRAD AGAIVAQLRI AIAPDDIAIT LHHKLCHAAR QLLEQTLPAI
KHGNILEIAQ RENEATCFGR RTPDDSFLEW HKPASVLHNM VRAVADPWPG AFSYVGNQKF
TVWSSRVHPH ASKAQPGSVI SVAPLLIACG DGALEIVTGQ AGDGITMQGS QLAQTLGLVQ
GSRLNSQPAC TARRRTRVLI LGVNGFIGNH LTERLLREDH YEVYGLDIGS DAISRFLNHP
HFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLRIIRYC
VKYRKRIIFP STSEVYGMCS DKYFDEDHSN LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK
EGLQFTLFRP FNWMGPRLDN LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI
RDGIEALYRI IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHHFPPFAGF
RVVESSSYYG KGYQDVEHRK PSIRNAHRCL DWEPKIDMQE TIDETLDFFL RTVDLTDKPS
