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Bifunctional polymyxin resistance protein ArnA [Includes: UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC 2.1.2.13) (ArnAFT) (UDP-L-Ara4N formyltransferase); UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating (EC 1.1.1.305) (ArnADH) (UDP-GlcUA decarboxylase) (UDP-glucuronic acid dehydrogenase)]

 ARNA_SALPB              Reviewed;         660 AA.
A9N5B2;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 1.
22-NOV-2017, entry version 79.
RecName: Full=Bifunctional polymyxin resistance protein ArnA {ECO:0000255|HAMAP-Rule:MF_01166};
Includes:
RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase {ECO:0000255|HAMAP-Rule:MF_01166};
EC=2.1.2.13 {ECO:0000255|HAMAP-Rule:MF_01166};
AltName: Full=ArnAFT {ECO:0000255|HAMAP-Rule:MF_01166};
AltName: Full=UDP-L-Ara4N formyltransferase {ECO:0000255|HAMAP-Rule:MF_01166};
Includes:
RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating {ECO:0000255|HAMAP-Rule:MF_01166};
EC=1.1.1.305 {ECO:0000255|HAMAP-Rule:MF_01166};
AltName: Full=ArnADH {ECO:0000255|HAMAP-Rule:MF_01166};
AltName: Full=UDP-GlcUA decarboxylase {ECO:0000255|HAMAP-Rule:MF_01166};
AltName: Full=UDP-glucuronic acid dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01166};
Name=arnA {ECO:0000255|HAMAP-Rule:MF_01166};
OrderedLocusNames=SPAB_00682;
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=1016998;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-1250 / SPB7;
The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V.,
Nash W., Johnson M., Thiruvilangam P., Wilson R.;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Bifunctional enzyme that catalyzes the oxidative
decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-
arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-
amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-
arabinose (UDP-L-Ara4FN). The modified arabinose is attached to
lipid A and is required for resistance to polymyxin and cationic
antimicrobial peptides. {ECO:0000255|HAMAP-Rule:MF_01166}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-
threo-pentapyranos-4-ulose + CO(2) + NADH. {ECO:0000255|HAMAP-
Rule:MF_01166}.
-!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + UDP-4-amino-4-
deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-
formamido-beta-L-arabinose. {ECO:0000255|HAMAP-Rule:MF_01166}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-
beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
arabinose from UDP-alpha-D-glucuronate: step 1/3.
{ECO:0000255|HAMAP-Rule:MF_01166}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-
beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
arabinose from UDP-alpha-D-glucuronate: step 3/3.
{ECO:0000255|HAMAP-Rule:MF_01166}.
-!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01166}.
-!- SUBUNIT: Homohexamer, formed by a dimer of trimers.
{ECO:0000255|HAMAP-Rule:MF_01166}.
-!- SIMILARITY: In the N-terminal section; belongs to the Fmt family.
UDP-L-Ara4N formyltransferase subfamily. {ECO:0000255|HAMAP-
Rule:MF_01166}.
-!- SIMILARITY: In the C-terminal section; belongs to the NAD(P)-
dependent epimerase/dehydratase family. UDP-glucuronic acid
decarboxylase subfamily. {ECO:0000255|HAMAP-Rule:MF_01166}.
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EMBL; CP000886; ABX66108.1; -; Genomic_DNA.
RefSeq; WP_000648753.1; NC_010102.1.
ProteinModelPortal; A9N5B2; -.
SMR; A9N5B2; -.
EnsemblBacteria; ABX66108; ABX66108; SPAB_00682.
KEGG; spq:SPAB_00682; -.
PATRIC; fig|1016998.12.peg.642; -.
HOGENOM; HOG000247761; -.
KO; K10011; -.
OMA; VRYCVKY; -.
UniPathway; UPA00030; -.
UniPathway; UPA00032; UER00492.
UniPathway; UPA00032; UER00494.
GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
GO; GO:0099619; F:UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0099618; F:UDP-glucuronic acid dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 3.10.25.10; -; 1.
Gene3D; 3.40.50.170; -; 1.
HAMAP; MF_01166; ArnA; 1.
InterPro; IPR021168; Bifun_polymyxin_resist_ArnA.
InterPro; IPR001509; Epimerase_deHydtase.
InterPro; IPR005793; Formyl_trans_C.
InterPro; IPR037022; Formyl_trans_C_sf.
InterPro; IPR002376; Formyl_transf_N.
InterPro; IPR036477; Formyl_transf_N_sf.
InterPro; IPR011034; Formyl_transferase-like_C_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01370; Epimerase; 1.
Pfam; PF02911; Formyl_trans_C; 1.
Pfam; PF00551; Formyl_trans_N; 1.
PIRSF; PIRSF036506; Bifun_polymyxin_resist_ArnA; 1.
SUPFAM; SSF50486; SSF50486; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF53328; SSF53328; 1.
3: Inferred from homology;
Antibiotic resistance; Lipid A biosynthesis; Lipid biosynthesis;
Lipid metabolism; Lipopolysaccharide biosynthesis;
Multifunctional enzyme; NAD; Oxidoreductase; Transferase.
CHAIN 1 660 Bifunctional polymyxin resistance protein
ArnA.
/FTId=PRO_1000085381.
NP_BIND 368 369 NAD binding. {ECO:0000255|HAMAP-
Rule:MF_01166}.
REGION 1 304 Formyltransferase ArnAFT.
REGION 136 140 10-formyltetrahydrofolate binding.
{ECO:0000255|HAMAP-Rule:MF_01166}.
REGION 314 660 Dehydrogenase ArnADH.
REGION 432 433 UDP-glucuronate binding.
{ECO:0000255|HAMAP-Rule:MF_01166}.
REGION 526 535 UDP-glucuronate binding.
{ECO:0000255|HAMAP-Rule:MF_01166}.
ACT_SITE 104 104 Proton donor; for formyltransferase
activity. {ECO:0000255|HAMAP-
Rule:MF_01166}.
ACT_SITE 434 434 Proton acceptor; for decarboxylase
activity. {ECO:0000255|HAMAP-
Rule:MF_01166}.
ACT_SITE 619 619 Proton donor; for decarboxylase activity.
{ECO:0000255|HAMAP-Rule:MF_01166}.
BINDING 114 114 10-formyltetrahydrofolate.
{ECO:0000255|HAMAP-Rule:MF_01166}.
BINDING 347 347 NAD. {ECO:0000255|HAMAP-Rule:MF_01166}.
BINDING 393 393 UDP-glucuronate; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01166}.
BINDING 398 398 UDP-glucuronate. {ECO:0000255|HAMAP-
Rule:MF_01166}.
BINDING 460 460 UDP-glucuronate. {ECO:0000255|HAMAP-
Rule:MF_01166}.
BINDING 492 492 UDP-glucuronate. {ECO:0000255|HAMAP-
Rule:MF_01166}.
BINDING 613 613 UDP-glucuronate. {ECO:0000255|HAMAP-
Rule:MF_01166}.
SITE 102 102 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01166}.
SITE 140 140 Raises pKa of active site His.
{ECO:0000255|HAMAP-Rule:MF_01166}.
SEQUENCE 660 AA; 73381 MW; DD209D984CDEDBEE CRC64;
MKAVIFAYHD MGCQGVQAVL DAGYDIAAIF THADNPAENT FFGSVSRLAA GLGIPVYAPD
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 AITQLILNLV EGTPIKLIDG GQQKRCFTDI
RDGIEALFRI IVNDGDRCDG KIINIGNPDN EASIQELATL LLDSFDKHPL RCHFPPFAGF
QVVESRSYYG KGYQDVAHRK PSIDNARRCL GWEPSIAMRD TVEETLDFFL RSVDVAERAS


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