2BLN,1Z7E


Conserved Protein Domain Family
Arna_FMT_C

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cd08702: Arna_FMT_C 
Click on image for an interactive view with Cn3D
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose
Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes 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). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.
Statistics
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PSSM-Id: 187730
Aligned: 35 rows
Threshold Bit Score: 93.8437
Created: 16-Apr-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitehexamer
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:The formyltrasferase active site is located primarily at the N-terminal subdomain of the ArnA formyltransferase-like domain.
  • Structure:2BLN_A; Escherichia coli ArnA complexed with the substrate mimics, N-5-Formyltetrahydrofolate and UMP; contact at 4A.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                            #    ##                                                     
2BLN_A       204 DDSFLEWHKPASVLHNMVRAVA-DPWPGAFSYVGNQKFTVWSSRVHPhas---kaQPGSVISv---APLLIACGd--GAL 274 Escherichia coli
Q8D341       205 KDGLIDWNQSANNIYNLIRALT-KPWPGAFSYLFDKKIIIWKSKISFes----ykTPGTILNf---NPLIISCKk--KSL 274 Wigglesworthia ...
ZP_06076427  204 LDGCIDWSNTAKDIDRLIKAST-SPHPGAFSFYGNNKVLVWKSNYYAsgy--akgVIGRVVNfn-nDNPVVQTAd--GYV 277 Bacteroides sp....
YP_003094196 198 KDGMINWNWQKERIKNWVRAQA-KPYPGAFSYVNDKKIIIHKVKFVDigfa-dndVNGEVISv--qEGIVVKTQn--GAL 271 Pedobacter hepa...
ZP_06439456  206 EDGKINWHWSGEEIYTLIRATS-KPYPGAFAYYKGKKVIFWKANLERnnk--yigIPGQIAKinnnGDLGIVTKg--SLL 280 Anaerobaculum s...
YP_003197490 200 EDGLINWEWPTSRIEGLVAALPlPKYPGAFTYFGNQKIVISKASAAEcpv--yycTPGQVVRitksGHAWIKTGdicLVV 277 Desulfohalobium...
YP_001788030 200 GDELIDWNWSSRRIHNFIRALV-EPAPGAQTYLNGDKICIWKSEETNfpd--yisTPGEIIRkd-kDGIIVKTGd--NAI 273 Clostridium bot...
YP_001782329 203 KDGIIDWRMSTEAILNLIKALT-KPYPGAEFEYNGQFITIWEATKYEcdkcynniEPGKVVKvi-gDCPIVKCYd--SLI 278 Clostridium bot...
ZP_01810703  199 GDEIINWIQSTREIFNFIRALN-TKDLGASAFIDEKEIKIYKSEIYKdki--fnaPIGKIVKke-kNFFIVSTKd--GAL 272 Campylobacter j...
ZP_01471754  184 GDEIIDWNQPSRSIFNFVRALS-TPGPNAQTFVGSNCIKIAKVELIDtapi-ykcIPGAILAkd-dNTFIVKTSd--SYL 258 Synechococcus s...
Feature 1                            
2BLN_A       275 EIVTGQAGd--GITMQGSQL 292 Escherichia coli
Q8D341       275 EILSAQYTe--CNILNKRNI 292 Wigglesworthia glossinidia endosymbiont of Glossina brevipalpis
ZP_06076427  278 ELVKYNMVdylDRPVDEHLV 297 Bacteroides sp. 2_1_33B
YP_003094196 272 MLIDYEVEg--SFNFEIGDI 289 Pedobacter heparinus DSM 2366
ZP_06439456  281 VVTEYSTEc-kNDNFSIGRK 299 Anaerobaculum sp. OS1
YP_003197490 278 QEVLIEGE---RNTKNAAEV 294 Desulfohalobium retbaense DSM 5692
YP_001788030 274 KIKLISYDg--DSKKVIPKI 291 Clostridium botulinum A3 str. Loch Maree
YP_001782329 279 KLVEYEPR---ITLKEGEYL 295 Clostridium botulinum B1 str. Okra
ZP_01810703  273 KITKFKGEvkiGYNFKIYTK 292 Campylobacter jejuni subsp. jejuni CG8486
ZP_01471754  259 RLLQWQCD---FKLAAGMRF 275 Synechococcus sp. RS9916

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