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ARNA_ECO81
ID   ARNA_ECO81              Reviewed;         660 AA.
AC   B7MXT6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=ECED1_2721;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR08902.2; -; Genomic_DNA.
DR   RefSeq; WP_000860302.1; NC_011745.1.
DR   AlphaFoldDB; B7MXT6; -.
DR   SMR; B7MXT6; -.
DR   EnsemblBacteria; CAR08902; CAR08902; ECED1_2721.
DR   KEGG; ecq:ECED1_2721; -.
DR   HOGENOM; CLU_007383_23_2_6; -.
DR   OMA; VRYCVKY; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00492.
DR   UniPathway; UPA00032; UER00494.
DR   Proteomes; UP000000748; 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   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_0000379987"
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;  74394 MW;  85253E0A52ECE753 CRC64;
     MKTVVFAYHD MGCLGIEALL SAGYEISAIF THTDNPGEKA FYGSVARLAA ERGIPVYAPD
     NVNHPLWMER IAQLSPEVIF SFYYRHLICD EILQLAPRGA FNLHGSLLPK YRGRAPLNWV
     LVNGETETGV TLHRMVKRAD AGAIVAQLRV AIAPDDIAIT LHHKLCHAAR QLLEQTLPAI
     KHGNILEIAQ RENEATCFGR RTPDDSFLEW HKPASVLHNM VRAVADPWPG AFSYVGNQKF
     TVWSSRVHPH ASKAQPGSVI SVAPLLIACG DGALEIVTGQ AGDGITMQGS QLAQTLGLVQ
     GSRLNSQPAC AARRRTRVLI LGVNGFIGNH LTERLLREDH YEVYGLDIGS DAISRFMNHP
     HFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLRIIRYC
     VKYRKRIIFP STSEVYGMCS DKYFDEDHSN LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK
     EGLQFTLFRP FNWMGPRLDN LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI
     RDGIEALYRI IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHYFPPFAGF
     RVVESSSYYG KGYQDVEHRK PSIRNARRCL NWEPKIDMQE TIDETLDFFL RTVDLTDKPS
 
 
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