ID A0A661LRV3_UNCDE Unreviewed; 295 AA. AC A0A661LRV3; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 24-JAN-2024, entry version 12. DE SubName: Full=Dihydropteroate synthase {ECO:0000313|EMBL:RLB28231.1}; GN ORFNames=DRG87_09770 {ECO:0000313|EMBL:RLB28231.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:RLB28231.1, ECO:0000313|Proteomes:UP000269286}; RN [1] {ECO:0000313|EMBL:RLB28231.1, ECO:0000313|Proteomes:UP000269286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B25_G16 {ECO:0000313|EMBL:RLB28231.1}; RA Dombrowski N., Teske A., Baker B.J.; RT "Extensive metabolic versatility and redundancy in microbially diverse, RT dynamic hydrothermal sediments."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase CC family. {ECO:0000256|ARBA:ARBA00010398}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RLB28231.1}. 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; QMLW01000249; RLB28231.1; -; Genomic_DNA. DR AlphaFoldDB; A0A661LRV3; -. DR Proteomes; UP000269286; Unassembled WGS sequence. DR GO; GO:0016740; F:transferase activity; IEA:UniProt. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding_dom. DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1. DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1. DR Pfam; PF00809; Pterin_bind; 1. DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 1..265 FT /note="Pterin-binding" FT /evidence="ECO:0000259|PROSITE:PS50972" SQ SEQUENCE 295 AA; 32863 MW; CEE3951E24B5A846 CRC64; MLLIGESLNV ISTKIGRAFK QKDPGPIQEE AKKQKELGMD FIDINLGPAR KGGPELMEWV IKTVQEVVDD VPLALDTSNI EAIEAGLSVY KGKEKALINS IMCRPERYEK MLPLCAKYNA AMIALLWGPH GMPRDENERG ELAVELVFAA NEAGIPNEDI YVDGIVTPVN VQQDQVYSLL QFMPMVKDIG EGLRSTCGLS NVSNGAPEHL RPILNQTYMV MLERLGMYSC IADAHDDKLV AIAKGKRPDI VEIIHKVMDD EEIDMGSVSK EMQDYVKTAR ILLKKSLYSD SWLEL //