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ARNA_SALG2
ID   ARNA_SALG2              Reviewed;         660 AA.
AC   B5RCC4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=SG2328;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR38158.1; -; Genomic_DNA.
DR   RefSeq; WP_000648765.1; NC_011274.1.
DR   AlphaFoldDB; B5RCC4; -.
DR   SMR; B5RCC4; -.
DR   EnsemblBacteria; CAR38158; CAR38158; SG2328.
DR   KEGG; seg:SG2328; -.
DR   HOGENOM; CLU_007383_23_2_6; -.
DR   OMA; VRYCVKY; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00492.
DR   UniPathway; UPA00032; UER00494.
DR   Proteomes; UP000008321; 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_1000137948"
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         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;  73440 MW;  DD1B9CD948D16488 CRC64;
     MKAVIFAYHD MGCQGVQAVL DAGYEIAAIF THADNPAENT FFGSVSRLAA ELGIPVYAPD
     NVNHPIWVDR IAELAPDIIF SFYYRNLLSE EILHLAPAGA FNLHGSLLPA YRGRAPLNWV
     LVNGESETGV TLHRMVKRAD AGEIVASQRV AIAQDDVALT LHHKLCQAAR QLLNSILPTM
     KCGDIPSVPQ RESDATYYGR RRPEDGLIDW HKPVSTVHNL VRAVAAPWPG AFSYNGSQKF
     TIWSSRICPD AQGALPGSVI SVSPLRVACA DGALEIITGQ AGDGITVQGS QLAQTLGLVA
     GARLNRPPAT SGKRRIRVLI LGVNGFIGNH LTERLLNEEN YEVYGMDIGS NAISRFLLHP
     RFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLRIIRYC
     VKYRKRVVFP STSEVYGMCT DASFDEDKSN LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK
     EGLRFTLFRP FNWMGPRLDS LNAARIGSSR AITQLILSLV EGTPIKLIDG GQQKRCFTDI
     RDGIEALFRI IVNDGDRCDG KIINIGNPDN EASIQELATL LLDSFDKHPL RCHFPPFAGF
     QVVESRSYYG KGYQDVAHRK PSIDNARRCL GWEPSIAMRD TVEETLDFFL RSVDVAERAS
 
 
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