Summary: Ethanolamine utilisation - propanediol utilisation
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Ethanolamine utilisation - propanediol utilisation Provide feedback
Members of this family function in ethanolamine and propanediol degradation pathways [1-3]. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments .
Sheppard DE, Penrod JT, Bobik T, Kofoid E, Roth JR; , J Bacteriol. 2004;186:7635-7644.: Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica. PUBMED:15516577 EPMC:15516577
Kofoid E, Rappleye C, Stojiljkovic I, Roth J; , J Bacteriol 1999;181:5317-5329.: The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. PUBMED:10464203 EPMC:10464203
Bobik TA, Havemann GD, Busch RJ, Williams DS, Aldrich HC; , J Bacteriol. 1999;181:5967-5975.: The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B(12)-dependent 1, 2-propanediol degradation. PUBMED:10498708 EPMC:10498708
Parsons JB, Frank S, Bhella D, Liang M, Prentice MB, Mulvihill DP, Warren MJ;, Mol Cell. 2010;38:305-315.: Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement. PUBMED:20417607 EPMC:20417607
Internal database links
|SCOOP:||AAA AAA_16 AAA_18 AAA_22 AAA_33 ABC_tran AIG1 Arf ATP_bind_1 cobW Dynamin_N FeoB_N GTP_EFTU Gtr1_RagA IIGP MMR_HSR1 MMR_HSR1_Xtn NOG1 Ras Roc RsgA_GTPase SRPRB|
|Similarity to PfamA using HHSearch:||AAA ABC_tran GTP_EFTU Arf Ras Dynamin_N SRP54 Septin RNA_helicase Mg_chelatase MMR_HSR1 FeoB_N ATP_bind_1 RsgA_GTPase RsgA_GTPase MobB Rad17 AIG1 Gtr1_RagA TniB NACHT AAA_5 Roc SRPRB MnmE_helical AAA_17 AAA_18 AAA_21 AAA_22 AAA_23 AAA_28 AAA_29 AAA_33|
This tab holds annotation information from the InterPro database.
InterPro entry IPR012381
Members of this family function in ethanolamine [ PUBMED:10464203 , PUBMED:26448059 ] and propanediol [ PUBMED:10498708 ] degradation pathways. Both pathways require coenzyme B12 (adenosylcobalamin, AdoCbl). Bacteria that harbour these pathways can use ethanolamine as a source of carbon and nitrogen, or propanediol as a sole carbon and energy source, respectively.
The exact roles of the EutP and PduV proteins in these respective pathways are not yet determined, however, EutP is a putative bidirectional acetate kinase that may drive flux through the ethanolamine degradation pathway under anoxic conditions found when Salmonella typhimurium infects host intestine. It may generate ATP that can be used by other enzymes (EutA and EutT) in the eut pathway. It can use GTP instead of ATP with reduced efficiency [ PUBMED:26448059 ]. Members of this family contain P-loop consensus motifs in the N-terminal part, and are distantly related to various GTPases and ATPases, including ATPase components of transport systems.
Propanediol degradation is thought to be important for the natural Salmonella populations, since propanediol is produced by the fermentation of the common plant sugars rhamnose and fucose [ PUBMED:10498708 , PUBMED:9023178 ]. More than 1% of the Salmonella enterica genome is devoted to the utilisation of propanediol and cobalamin biosynthesis. In vivo expression technology has indicated that propanediol utilisation ( pdu ) genes may be important for growth in host tissues, and competitive index studies with mice have shown that pdu mutations confer a virulence defect [ PUBMED:9539791 , PUBMED:9922242 ]. The pdu operon is contiguous and co-regulated with the cobalamin (B12) biosynthesis cob operon, indicating that propanediol catabolism may be the primary reason for de novo B12 synthesis in Salmonella [ PUBMED:1312999 , PUBMED:8226666 , PUBMED:1313000 ].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||ATP binding (GO:0005524)|
|Biological process||cellular biogenic amine metabolic process (GO:0006576)|
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AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes .
The clan contains the following 245 members:6PF2K AAA AAA-ATPase_like AAA_10 AAA_11 AAA_12 AAA_13 AAA_14 AAA_15 AAA_16 AAA_17 AAA_18 AAA_19 AAA_2 AAA_21 AAA_22 AAA_23 AAA_24 AAA_25 AAA_26 AAA_27 AAA_28 AAA_29 AAA_3 AAA_30 AAA_31 AAA_32 AAA_33 AAA_34 AAA_35 AAA_5 AAA_6 AAA_7 AAA_8 AAA_9 AAA_PrkA ABC_ATPase ABC_tran ABC_tran_Xtn Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arf ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 ATPase ATPase_2 Bac_DnaA BCA_ABC_TP_C Beta-Casp bpMoxR BrxC_BrxD BrxL_ATPase Cas_Csn2 Cas_St_Csn2 CbiA CBP_BcsQ CDC73_C CENP-M CFTR_R CLP1_P CMS1 CoaE CobA_CobO_BtuR CobU cobW CPT CSM2 CTP_synth_N Cytidylate_kin Cytidylate_kin2 DAP3 DEAD DEAD_2 divDNAB DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DNA_pol3_delta2 DnaB_C dNK DO-GTPase1 DO-GTPase2 DUF1611 DUF2075 DUF2326 DUF2478 DUF257 DUF2813 DUF3584 DUF463 DUF4914 DUF5906 DUF6079 DUF815 DUF835 DUF87 DUF927 Dynamin_N Dynein_heavy Elong_Iki1 ELP6 ERCC3_RAD25_C Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GBP_C GpA_ATPase GpA_nuclease GTP_EFTU Gtr1_RagA Guanylate_kin GvpD_P-loop HDA2-3 Helicase_C Helicase_C_2 Helicase_C_4 Helicase_RecD HerA_C Herpes_Helicase Herpes_ori_bp Herpes_TK HydF_dimer HydF_tetramer Hydin_ADK IIGP IPPT IPT iSTAND IstB_IS21 KAP_NTPase KdpD Kinase-PPPase Kinesin KTI12 LAP1_C LpxK MCM MeaB MEDS Mg_chelatase Microtub_bd MipZ MMR_HSR1 MMR_HSR1_C MobB MukB Mur_ligase_M MutS_V Myosin_head NACHT NAT_N NB-ARC NOG1 NTPase_1 NTPase_P4 ORC3_N P-loop_TraG ParA Parvo_NS1 PAXNEB PduV-EutP PhoH PIF1 Ploopntkinase1 Ploopntkinase2 Ploopntkinase3 Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK PSY3 Rad17 Rad51 Ras RecA ResIII RHD3_GTPase RhoGAP_pG1_pG2 RHSP RNA12 RNA_helicase Roc RsgA_GTPase RuvB_N SbcC_Walker_B SecA_DEAD Senescence Septin Sigma54_activ_2 Sigma54_activat SKI SMC_N SNF2-rel_dom SpoIVA_ATPase Spore_III_AA SRP54 SRPRB SulA Sulfotransfer_1 Sulfotransfer_2 Sulfotransfer_3 Sulfotransfer_4 Sulfotransfer_5 Sulphotransf SWI2_SNF2 T2SSE T4SS-DNA_transf TerL_ATPase Terminase_3 Terminase_6N Thymidylate_kin TIP49 TK TmcA_N TniB Torsin TraG-D_C tRNA_lig_kinase TrwB_AAD_bind TsaE UvrB UvrD-helicase UvrD_C UvrD_C_2 Viral_helicase1 VirC1 VirE YqeC Zeta_toxin Zot
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Seed source:||FIG047026 (Release 2.0)|
|Author:||FIGfams, Mistry J , Coggill P|
|Number in seed:||15|
|Number in full:||586|
|Average length of the domain:||138.5 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||84.5 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
|Protein||Predicted structure||External Information|
|A0A0H3GTF9||View 3D Structure||Click here|
|A0A0H3GX16||View 3D Structure||Click here|
|P0A208||View 3D Structure||Click here|
|P76556||View 3D Structure||Click here|
|Q2EES3||View 3D Structure||Click here|
|Q8X8U4||View 3D Structure||Click here|
|Q9XDM6||View 3D Structure||Click here|
The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.
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