ID A0A0M9GI66_9PSED Unreviewed; 663 AA.
AC A0A0M9GI66;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=PF66_01451 {ECO:0000313|EMBL:KPA91869.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA91869.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA91869.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA91869.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
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:KPA91869.1}.
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DR EMBL; JSYZ01000004; KPA91869.1; -; Genomic_DNA.
DR RefSeq; WP_054062268.1; NZ_JSYZ01000004.1.
DR AlphaFoldDB; A0A0M9GI66; -.
DR STRING; 50340.PF66_01451; -.
DR PATRIC; fig|50340.43.peg.4606; -.
DR OrthoDB; 9802815at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00492.
DR Proteomes; UP000037931; 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:KPA91869.1}.
FT DOMAIN 27..178
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 205..284
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT DOMAIN 321..568
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT REGION 1..307
FT /note="Formyltransferase ArnAFT"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT REGION 317..663
FT /note="Dehydrogenase ArnADH"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT ACT_SITE 106
FT /note="Proton donor; for formyltransferase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT ACT_SITE 437
FT /note="Proton acceptor; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT ACT_SITE 621
FT /note="Proton donor; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 116
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 138..142
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 350
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 371..372
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 396
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 401
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 435..436
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 463
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 494
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 528..537
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT BINDING 615
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT SITE 104
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
FT SITE 142
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01166"
SQ SEQUENCE 663 AA; 73962 MW; 4144773EE5D2D99A CRC64;
MNPKAVVFAY HDIGCAGIEA LLNAGYEIAA VFTHADDPKE NTFYGSVAQL CALKGIPVHA
PEDANHPLWI ERIAKLNPDF IFSFYYRNLL SEALLATAKN GAFNLHGSLL PRYRGRAPAN
WVLVNGETET GVTLHRMVKR ADAGAILAQN RVAIERSDTA LSLHAKLRDS AASLLRDALP
QLAQGKLSET AQDESKATYF GRRTAADGKL VWSKPAEELF NLIRAVTKPY PGAFCAVGEH
KLIVWGAEVV KGNEGQAPGR VISVDPLRIA CGEDSLVINA GQRNENGLFL SGPQLANELG
LVDGSLLRGA EAARKKRRTR VLILGVNGFI GNHLSERLLR DDKYEVYGLD IGSDAIERLR
SHPNFHFVEG DISIHSEWIE YHIKKCDVVL PLVAIATPIE YTRNPLRVFE LDFEENLKLV
RYCVKYNKRV IFPSTSEVYG MCQDKNFDED TSNLIVGPIS KQRWIYSVSK QLLDRVIWAY
GAKGLNFTLF RPFNWMGPRL DRLDSARIGS SRAITQLILN LVEGTPIRLF DGGEQKRCFT
DIADGIEALA RIVDNENDCC NGQIINIGNP DNEASIRQLG EELLRQFEAH PLRGNFPPFA
GFREVESKAF YGAGYQDVEH RKPSIENAKR LLNWEPTVEM SETIGNTLDF FLKEAMLEIA
EKR
//
