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

 A0A1N6MYL8_9GAMM        Unreviewed;       671 AA.
A0A1N6MYL8;
15-MAR-2017, integrated into UniProtKB/TrEMBL.
15-MAR-2017, sequence version 1.
22-NOV-2017, entry version 7.
RecName: Full=Bifunctional polymyxin resistance protein ArnA {ECO:0000256|HAMAP-Rule:MF_01166};
Includes:
RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating {ECO:0000256|HAMAP-Rule:MF_01166};
EC=1.1.1.305 {ECO:0000256|HAMAP-Rule:MF_01166};
AltName: Full=UDP-GlcUA decarboxylase {ECO:0000256|HAMAP-Rule:MF_01166};
AltName: Full=UDP-glucuronic acid dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01166};
AltName: Full=ArnADH {ECO:0000256|HAMAP-Rule:MF_01166};
Includes:
RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase {ECO:0000256|HAMAP-Rule:MF_01166};
EC=2.1.2.13 {ECO:0000256|HAMAP-Rule:MF_01166};
AltName: Full=UDP-L-Ara4N formyltransferase {ECO:0000256|HAMAP-Rule:MF_01166};
AltName: Full=ArnAFT {ECO:0000256|HAMAP-Rule:MF_01166};
Name=pbgP {ECO:0000313|EMBL:SIP73945.1};
Synonyms=arnA {ECO:0000256|HAMAP-Rule:MF_01166};
ORFNames=XIS1_480071 {ECO:0000313|EMBL:SIP73945.1};
Xenorhabdus innexi.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Morganellaceae; Xenorhabdus.
NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP73945.1, ECO:0000313|Proteomes:UP000196435};
[1] {ECO:0000313|EMBL:SIP73945.1, ECO:0000313|Proteomes:UP000196435}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
Collection) {ECO:0000313|Proteomes:UP000196435};
Song W.-J., Kurnit D.M.;
Submitted (DEC-2016) 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:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930012}.
-!- 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:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930196}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-
threo-pentapyranos-4-ulose + CO(2) + NADH. {ECO:0000256|HAMAP-
Rule:MF_01166, ECO:0000256|SAAS:SAAS00930065}.
-!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930195}.
-!- 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:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930158}.
-!- 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:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930003}.
-!- SUBUNIT: Homohexamer, formed by a dimer of trimers.
{ECO:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930146}.
-!- SIMILARITY: In the C-terminal section; belongs to the NAD(P)-
dependent epimerase/dehydratase family. UDP-glucuronic acid
decarboxylase subfamily. {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930110}.
-!- SIMILARITY: In the N-terminal section; belongs to the Fmt family.
UDP-L-Ara4N formyltransferase subfamily. {ECO:0000256|HAMAP-
Rule:MF_01166, ECO:0000256|SAAS:SAAS00930013}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01166}.
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EMBL; FTLG01000190; SIP73945.1; -; Genomic_DNA.
UniPathway; UPA00030; -.
UniPathway; UPA00032; UER00492.
UniPathway; UPA00032; UER00494.
Proteomes; UP000196435; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930186};
Complete proteome {ECO:0000313|Proteomes:UP000196435};
Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930035};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930035};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930035};
Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930194};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930103};
NAD {ECO:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930009};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930032};
Reference proteome {ECO:0000313|Proteomes:UP000196435};
Transferase {ECO:0000256|HAMAP-Rule:MF_01166,
ECO:0000256|SAAS:SAAS00930026, ECO:0000313|EMBL:SIP73945.1}.
DOMAIN 57 173 Formyl_trans_N.
{ECO:0000259|Pfam:PF00551}.
DOMAIN 203 283 Formyl_trans_C.
{ECO:0000259|Pfam:PF02911}.
DOMAIN 318 566 Epimerase. {ECO:0000259|Pfam:PF01370}.
NP_BIND 368 369 NAD binding. {ECO:0000256|HAMAP-
Rule:MF_01166}.
REGION 1 304 Formyltransferase ArnAFT.
{ECO:0000256|HAMAP-Rule:MF_01166}.
REGION 314 671 Dehydrogenase ArnADH. {ECO:0000256|HAMAP-
Rule:MF_01166}.
REGION 432 433 UDP-glucuronate binding.
{ECO:0000256|HAMAP-Rule:MF_01166}.
REGION 526 535 UDP-glucuronate binding.
{ECO:0000256|HAMAP-Rule:MF_01166}.
ACT_SITE 104 104 Proton donor; for formyltransferase
activity. {ECO:0000256|HAMAP-
Rule:MF_01166}.
ACT_SITE 434 434 Proton acceptor; for decarboxylase
activity. {ECO:0000256|HAMAP-
Rule:MF_01166}.
ACT_SITE 619 619 Proton donor; for decarboxylase activity.
{ECO:0000256|HAMAP-Rule:MF_01166}.
BINDING 114 114 10-formyltetrahydrofolate.
{ECO:0000256|HAMAP-Rule:MF_01166}.
BINDING 347 347 NAD. {ECO:0000256|HAMAP-Rule:MF_01166}.
BINDING 393 393 UDP-glucuronate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01166}.
BINDING 398 398 UDP-glucuronate. {ECO:0000256|HAMAP-
Rule:MF_01166}.
BINDING 460 460 UDP-glucuronate. {ECO:0000256|HAMAP-
Rule:MF_01166}.
BINDING 492 492 UDP-glucuronate. {ECO:0000256|HAMAP-
Rule:MF_01166}.
BINDING 613 613 UDP-glucuronate. {ECO:0000256|HAMAP-
Rule:MF_01166}.
SITE 102 102 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01166}.
SITE 140 140 Raises pKa of active site His.
{ECO:0000256|HAMAP-Rule:MF_01166}.
SEQUENCE 671 AA; 75548 MW; 75084F45ED93BA9B CRC64;
MKAVIFAYHD IGCTGLNALM KAGFDIRAIF THADDPNENN FFSSVARAGA DLGLSVFAPE
NVNHPLWVER IREMQPDIIF SFYYRNMLSQ DILSLAKKGA FNLHGSLLPK YRGRAPVNWA
VLNGETKTGV TLHKMSVKAD AGDIVAQQAV QIEKTDTSLI VHGKIREAAI ELLDDILPRL
KADNYTSIPQ DESQATYFGR RAAEDGEIFW HKSAEEINNL VRAVTEPYPG AFTFLGERKI
TIWRSAPLNK THGKQAGTVL SIDPLVIACG TGALEIVTGQ SETGIYVQGG RLAQEMGIVT
EVQVGQKATA QFPRRKRVLI LGVNGFIGNH LTERLLNDGN YDIYGMDIGS SAIERFIGNP
HFHFIEGDVS IHTEWIEYHI KKCDVILPLV AIATPIEYTR NPLRVFELDF EENLKIVRYC
VKYNKRIIFP STSEVYGMCD DKEFDEDTSR LIVGPINKQR WIYSVSKQLL DRVIWAYGEK
EGLKFTLFRP FNWMGPRLDN LNSARIGSSR AITQLILNLV EGSPIKLVDG GEQKRCFTDI
NDGIDALFRI IENKNGLCDG RIINIGNPTN EASIRQLAEI LLNSFEKHEL RGHFPPFAGF
KKIESSSYYG QGYQDVEHRK PSIKNAARLL GWKPTIGMEQ TVDETLDFFL RDAVQELNRK
KKHTEHIPDG F


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