ID A0A1V9DLR9_9GAMM Unreviewed; 659 AA.
AC A0A1V9DLR9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Bifunctional polymyxin resistance protein ArnA {ECO:0000256|HAMAP-Rule:MF_01166};
DE Includes:
DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase {ECO:0000256|HAMAP-Rule:MF_01166};
DE EC=2.1.2.13 {ECO:0000256|HAMAP-Rule:MF_01166};
DE AltName: Full=ArnAFT {ECO:0000256|HAMAP-Rule:MF_01166};
DE AltName: Full=UDP-L-Ara4N formyltransferase {ECO:0000256|HAMAP-Rule:MF_01166};
DE Includes:
DE RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating {ECO:0000256|HAMAP-Rule:MF_01166};
DE EC=1.1.1.305 {ECO:0000256|HAMAP-Rule:MF_01166};
DE AltName: Full=ArnADH {ECO:0000256|HAMAP-Rule:MF_01166};
DE AltName: Full=UDP-GlcUA decarboxylase {ECO:0000256|HAMAP-Rule:MF_01166};
DE AltName: Full=UDP-glucuronic acid dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01166};
GN Name=arnA {ECO:0000256|HAMAP-Rule:MF_01166};
GN ORFNames=B2J69_08195 {ECO:0000313|EMBL:OQP34780.1};
OS Pantoea latae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1964541 {ECO:0000313|EMBL:OQP34780.1, ECO:0000313|Proteomes:UP000192769};
RN [1] {ECO:0000313|EMBL:OQP34780.1, ECO:0000313|Proteomes:UP000192769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS1 {ECO:0000313|EMBL:OQP34780.1,
RC ECO:0000313|Proteomes:UP000192769};
RA Lata P., Govindarajan S., Qi F., Li J.-L., Maurya S.K., Sahoo M.K.;
RT "Whole genome shotgun sequence of Pantoea agglomerans strain AS1 isolated
RT from a cycad, Zamia floridana in Central Florida, USA.";
RL Submitted (FEB-2017) 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:0000256|HAMAP-Rule:MF_01166}.
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; Evidence={ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-
CC Rule:MF_01166};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000256|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 1/3. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01166}.
CC -!- SUBUNIT: Homohexamer, formed by a dimer of trimers. {ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_01166}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the Fmt family. UDP-
CC L-Ara4N formyltransferase subfamily. {ECO:0000256|HAMAP-Rule:MF_01166}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01166}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQP34780.1}.
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DR EMBL; MWUE01000011; OQP34780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9DLR9; -.
DR OrthoDB; 9802815at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00492.
DR Proteomes; UP000192769; Unassembled WGS sequence.
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 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 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 Pfam; PF00551; Formyl_trans_N; 1.
DR PIRSF; PIRSF036506; Bifun_polymyxin_resist_ArnA; 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 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW Rule:MF_01166};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_01166};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01166};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01166};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW ECO:0000256|HAMAP-Rule:MF_01166};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01166};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01166};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01166};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01166, ECO:0000313|EMBL:OQP34780.1}.
FT DOMAIN 47..175
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 202..295
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT DOMAIN 318..566
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT REGION 1..304
FT /note="Formyltransferase ArnAFT"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..659
FT /note="Dehydrogenase ArnADH"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT ACT_SITE 104
FT /note="Proton donor; for formyltransferase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT ACT_SITE 434
FT /note="Proton acceptor; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT ACT_SITE 619
FT /note="Proton donor; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 114
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 136..140
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 368..369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 393
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 398
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 432..433
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 460
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 492
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 526..535
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 613
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT SITE 102
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT SITE 140
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
SQ SEQUENCE 659 AA; 73482 MW; 17C73936078D9E89 CRC64;
MKTIVFAYAE MGCAGITALL NAGYEIGAIF THADTSPESH AFPSVARLAA EHGIPVYAPE
DASHPLWVDR IRAMQPDVIF SFYYRALLSS TLLDCARIGA FNLHGSLLPK YRGRAPLNWV
LVNGETETGV TLHRMVKRAD AGDIVAQQRV AIDEQDNALT LHRKLVACAA QLLESALPAI
KRGEIAATPQ NEAEATKVGR RTPEDGRIDW TRPAQAINNL VRAVTDPWPG AFAFAGTVKF
VVWKGRVHSD APQAKPGTVL SVAPFLIACG EGALEVVTGQ SDNGVYMNGS QLAQSLGMVP
GALLYSQPVA AVKRRTRVLI LGVNGFIGNH LTERLLQDDN FDVYGLDIGS DAISRFLEQP
RFHFVEGDIS IHSEWIEYHI KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLKIIRDC
VKYKKRIIFP STSEVYGMCT DAHFDEDHSN LVVGPINKQR WIYSVSKQLL DRVIWAYGEK
EGLRFTLFRP FNWMGPRLDN LNAARIGSSR AITQLILNLV EGSPIKLIDG GAQKRCFTDI
RDGIEALFRI IENKNNNCDG QIVNIGNPDN EASIKELAER LLASFERHPL RDRFPPFAGF
REVESSSYYG KGYQDVEHRK PSIKNARRLL AWTPTVEMDT TIDNTLDFFL RTVELQDKP
//
