Conserved Protein Domain Family
Pro_3_hydrox_C

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pfam05373: Pro_3_hydrox_C 
L-proline 3-hydroxylase, C-terminal
Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalyzing oxidation of a free alpha-amino acid. The structure contains conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. The structure differs significantly from many other 2-OG oxygenases in possessing a discrete C-terminal helical domain.
Statistics
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PSSM-Id: 398832
Aligned: 3 rows
Threshold Bit Score: 163.556
Threshold Setting Gi: 502653955
Created: 11-May-2020
Updated: 7-Aug-2020
Structure
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Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
WP_015402230 182 EASIFRDLSsyQPDLSPEIRE-RAAFTSDLEQRLLRLSEVVNRRNFKDVLFLLSKIHFDYNVPGERTYDWLLDICRTAGD 260 Corynebacterium...
Q92LF6       177 PESFLRNVE--QPVTTRDMVDpRKELTDEVIEGILGFSIIISEANYREIVSILAKLHFFYKADCRSMYDWLKEICKRRGD 254 Sinorhizobium m...
WP_012890182 188 RAGd------yDPAIRPALVE-RAPAPADLPDRLRALSAVVSRHNIKDIAFLLGKVHFTEEVPIGASWDWLVEITRASGD 260 Streptosporangi...
WP_015402230 261 DQLIAKAEMVRDYMINVRALGE 282 Corynebacterium halotolerans
Q92LF6       255 PALIEKTASLERFFLGHRERGE 276 Sinorhizobium meliloti 1021
WP_012890182 261 PALLDLAERARRFFVHSREVYE 282 Streptosporangium roseum
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