ID A0A085GAK7_9GAMM Unreviewed; 660 AA. AC A0A085GAK7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 20-DEC-2017, entry version 26. DE RecName: Full=Bifunctional polymyxin resistance protein ArnA {ECO:0000256|HAMAP-Rule:MF_01166}; DE Includes: DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase {ECO:0000256|HAMAP-Rule:MF_01166}; DE EC=2.1.2.13 {ECO:0000256|HAMAP-Rule:MF_01166}; DE AltName: Full=ArnAFT {ECO:0000256|HAMAP-Rule:MF_01166}; DE AltName: Full=UDP-L-Ara4N formyltransferase {ECO:0000256|HAMAP-Rule:MF_01166}; DE Includes: DE RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating {ECO:0000256|HAMAP-Rule:MF_01166}; DE EC=1.1.1.305 {ECO:0000256|HAMAP-Rule:MF_01166}; DE AltName: Full=UDP-glucuronic acid dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01166}; DE AltName: Full=UDP-GlcUA decarboxylase {ECO:0000256|HAMAP-Rule:MF_01166}; DE AltName: Full=ArnADH {ECO:0000256|HAMAP-Rule:MF_01166}; GN Name=arnA {ECO:0000256|HAMAP-Rule:MF_01166}; GN ORFNames=GEAM_2074 {ECO:0000313|EMBL:KFC80752.1}; OS Ewingella americana ATCC 33852. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Ewingella. OX NCBI_TaxID=910964 {ECO:0000313|EMBL:KFC80752.1, ECO:0000313|Proteomes:UP000028640}; RN [1] {ECO:0000313|EMBL:KFC80752.1, ECO:0000313|Proteomes:UP000028640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33852 {ECO:0000313|EMBL:KFC80752.1, RC ECO:0000313|Proteomes:UP000028640}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction RT of the evolutionary history of the Enterobacteriaceae."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. 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 CC lipid A and is required for resistance to polymyxin and cationic CC antimicrobial peptides. {ECO:0000256|HAMAP-Rule:MF_01166, CC ECO:0000256|SAAS:SAAS00930012}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + UDP-4-amino-4- CC deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4- CC formamido-beta-L-arabinose. {ECO:0000256|HAMAP-Rule:MF_01166, CC ECO:0000256|SAAS:SAAS00930196}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L- CC threo-pentapyranos-4-ulose + CO(2) + NADH. {ECO:0000256|HAMAP- CC Rule:MF_01166, ECO:0000256|SAAS:SAAS00930065}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01166, CC ECO:0000256|SAAS:SAAS00930195}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido- CC beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L- CC arabinose from UDP-alpha-D-glucuronate: step 1/3. CC {ECO:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930158}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido- CC beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L- CC arabinose from UDP-alpha-D-glucuronate: step 3/3. CC {ECO:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930003}. CC -!- SUBUNIT: Homohexamer, formed by a dimer of trimers. CC {ECO:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930146}. CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD(P)- CC dependent epimerase/dehydratase family. UDP-glucuronic acid CC decarboxylase subfamily. {ECO:0000256|HAMAP-Rule:MF_01166, CC ECO:0000256|SAAS:SAAS00930110}. CC -!- SIMILARITY: In the N-terminal section; belongs to the Fmt family. CC UDP-L-Ara4N formyltransferase subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01166, ECO:0000256|SAAS:SAAS00930013}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01166}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC80752.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JMPJ01000053; KFC80752.1; -; Genomic_DNA. DR RefSeq; WP_034791177.1; NZ_JMPJ01000053.1. DR EnsemblBacteria; KFC80752; KFC80752; GEAM_2074. DR UniPathway; UPA00030; -. DR UniPathway; UPA00032; UER00492. DR Proteomes; UP000028640; Unassembled WGS sequence. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. 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 Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_01166; ArnA; 1. DR InterPro; IPR021168; Bifun_polymyxin_resist_ArnA. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR037022; Formyl_trans_C_sf. 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 {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930186}; KW Complete proteome {ECO:0000313|Proteomes:UP000028640}; KW Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930035}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930034}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930198}; KW Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930194}; Lyase {ECO:0000313|EMBL:KFC80752.1}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930103}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01166, ECO:0000256|SAAS:SAAS00930009}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930032}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01166, KW ECO:0000256|SAAS:SAAS00930026, ECO:0000313|EMBL:KFC80752.1}. FT DOMAIN 53 176 Formyl_trans_N. {ECO:0000259|Pfam: FT PF00551}. FT DOMAIN 203 284 Formyl_trans_C. {ECO:0000259|Pfam: FT PF02911}. FT DOMAIN 318 566 Epimerase. {ECO:0000259|Pfam:PF01370}. FT NP_BIND 368 369 NAD binding. {ECO:0000256|HAMAP-Rule: FT MF_01166}. FT REGION 1 304 Formyltransferase ArnAFT. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT REGION 136 140 10-formyltetrahydrofolate binding. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT REGION 314 660 Dehydrogenase ArnADH. {ECO:0000256|HAMAP- FT Rule:MF_01166}. FT REGION 432 433 UDP-glucuronate binding. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT REGION 526 535 UDP-glucuronate binding. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT ACT_SITE 104 104 Proton donor; for formyltransferase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01166}. FT ACT_SITE 434 434 Proton acceptor; for decarboxylase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01166}. FT ACT_SITE 619 619 Proton donor; for decarboxylase activity. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT BINDING 114 114 10-formyltetrahydrofolate. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT BINDING 347 347 NAD. {ECO:0000256|HAMAP-Rule:MF_01166}. FT BINDING 393 393 UDP-glucuronate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT BINDING 398 398 UDP-glucuronate. {ECO:0000256|HAMAP-Rule: FT MF_01166}. FT BINDING 460 460 UDP-glucuronate. {ECO:0000256|HAMAP-Rule: FT MF_01166}. FT BINDING 492 492 UDP-glucuronate. {ECO:0000256|HAMAP-Rule: FT MF_01166}. FT BINDING 613 613 UDP-glucuronate. {ECO:0000256|HAMAP-Rule: FT MF_01166}. FT SITE 102 102 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01166}. FT SITE 140 140 Raises pKa of active site His. FT {ECO:0000256|HAMAP-Rule:MF_01166}. SQ SEQUENCE 660 AA; 74119 MW; 2F5C877736ED6566 CRC64; MKAIVFAYHD IGCVGLQALV DAGYDVQAVF THTDSPDENN FFSSVARVGA GLNLPVYAPE DVNHPLWVDR IRELQPDVIF SFYYRNMLSE EVLSLAPLGG FNLHGSLLPR YRGRAPVNWA LLKGETETGV TLHKMVKRPD AGDIVGQLAV PISNDDIALT LHAKVRDAAK VLLTDVLPKI KQGNVTLTPQ DESQASYFGR RTAADGEIHW HKSATEINNL IRAVTEPYPG AFTYLGQRKM TIWRSRPLDT AHDKKPGTVL SSDPLVVACG TGALEILAGQ SESGLYVQGS RLALELGIMP DVKLSSLPTA VMKRRTRVLI LGVNGFIGNH LSERLLREDN YEIFGLDISS DAVSRFMDNP HFHFVEGDIS IHSEWIEYHI KKCDVILPLV AIATPIEYTR NPLRVFELDF EENLKIVRDC VKYKKRIIFP STSEVYGMCD DKEFDEDTSR LIVGPINKQR WIYSVSKQLL DRVIWAYGVK EGLRFTLFRP FNWMGPRLDN LDAARIGSSR AITQLILNLV EGSPIKLVDG GEQKRTFTDI TDGIEALFRI VENKEDRCDG QIINIGNPTN EASIRELAEM LLRSFEAHPL RDQFPPFAGF KSVESSTYYG KGYQDVEHRT PSIKNAKRLL GWTPEIAMDK TVEKTLDFFL RSVNPDNNQA //