ID ARNA_WIGBR Reviewed; 654 AA.
AC Q8D341;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 130.
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=WIGBR1600;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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=(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: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; BA000021; BAC24306.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8D341; -.
DR SMR; Q8D341; -.
DR STRING; 36870.gene:10368648; -.
DR KEGG; wbr:b2255; -.
DR eggNOG; COG0223; Bacteria.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_23_1_6; -.
DR OrthoDB; 9802815at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00492.
DR UniPathway; UPA00032; UER00494.
DR Proteomes; UP000000562; 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 CDD; cd08644; FMT_core_ArnA_N; 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; IPR001555; GART_AS.
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; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW NAD; Oxidoreductase; Reference proteome; Transferase.
FT CHAIN 1..654
FT /note="Bifunctional polymyxin resistance protein ArnA"
FT /id="PRO_0000083111"
FT REGION 1..303
FT /note="Formyltransferase ArnAFT"
FT REGION 313..654
FT /note="Dehydrogenase ArnADH"
FT ACT_SITE 105
FT /note="Proton donor; for formyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT ACT_SITE 433
FT /note="Proton acceptor; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT ACT_SITE 618
FT /note="Proton donor; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 137..141
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 367..368
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 392
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 397
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 431..432
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 459
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 491
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 532..534
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT BINDING 612
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT SITE 103
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
FT SITE 141
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01166"
SQ SEQUENCE 654 AA; 76367 MW; 2C3B783A90C8BCB2 CRC64;
MKVIVFAYHE IGYIGLSCLI KLGFKVLSVI THIDDHASEK IFFSSVKKKS LKHKIPVFYP
KNINNLKWID YLSKLKPDII FSFYYRKILS EDILKIPKLG SFNLHGSLLP KYRGCSPLNW
VLINGEKTTG VTLHRMTKKI DHGSILSQYS IKIEEKDTSK SLYKKLCYAS MYILNKTLPM
ILKNKINEID CTDDFSSYFH KRYPKDGLID WNQSANNIYN LIRALTKPWP GAFSYLFDKK
IIIWKSKISF ESYKTPGTIL NFNPLIISCK KKSLEILSAQ YTECNILNKR NIENISRIKG
KKLIIKNIKS FKNLKKILIL GVNGFIGYHI TNLLLKYNNY KIYGIDIKNN LVKSFIGNEK
FCFIKGDIKQ YYNWVKKKIK KCDIILPLIA IARPMQYIKN PLKVFKIDFE ENLKIIRYCV
KYKKRIIFPS TSEVYGMCKD DYFDEENSNL VTGAIKNQRW IYSSSKQLLD RIIWAYGVKN
NLNFTIFRPF NWIGPGLDDF KIAEKQNARV TTQIIFNLIN GLPVTIVNNG NQKRCFTDID
DGIEALFEII KNKNNKCNKK IINIGNPHNE YTIMQLTKII INIIYSNNRN YNFPKFSGFN
MLSGTNYYGE GYQDIDRRKP NIDIAKKLLN WTPKTKIRIT LRKIINFFIN NNTS
//
