ID E1R9Y5_SEDSS Unreviewed; 540 AA. AC E1R9Y5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 58. DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063}; DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063}; GN OrderedLocusNames=Spirs_4230 {ECO:0000313|EMBL:ADK83304.1}; OS Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228) OS (Spirochaeta smaragdinae). OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae; OC Sediminispirochaeta. OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK83304.1, ECO:0000313|Proteomes:UP000002318}; RN [1] {ECO:0000313|EMBL:ADK83304.1, ECO:0000313|Proteomes:UP000002318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228 RC {ECO:0000313|Proteomes:UP000002318}; RX PubMed=21304743; DOI=10.4056/sigs.1143106; RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M., RA Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., RA Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M., RA Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR RT 4228)."; RL Stand. Genomic Sci. 3:136-144(2010). CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP CC mutase family. {ECO:0000256|ARBA:ARBA00038455}. 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; CP002116; ADK83304.1; -; Genomic_DNA. DR RefSeq; WP_013256760.1; NC_014364.1. DR AlphaFoldDB; E1R9Y5; -. DR STRING; 573413.Spirs_4230; -. DR KEGG; ssm:Spirs_4230; -. DR eggNOG; COG1213; Bacteria. DR eggNOG; COG2513; Bacteria. DR HOGENOM; CLU_544759_0_0_12; -. DR OrthoDB; 8629576at2; -. DR Proteomes; UP000002318; Chromosome. DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC. DR CDD; cd00377; ICL_PEPM; 1. DR CDD; cd02523; PC_cytidylyltransferase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR InterPro; IPR039556; ICL/PEPM. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR012698; PEnolPyrv_PMutase_core. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf. DR NCBIfam; TIGR02320; PEP_mutase; 1. DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1. DR Pfam; PF12804; NTP_transf_3; 1. DR Pfam; PF13714; PEP_mutase; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}; KW Reference proteome {ECO:0000313|Proteomes:UP000002318}. FT DOMAIN 298..421 FT /note="MobA-like NTP transferase" FT /evidence="ECO:0000259|Pfam:PF12804" SQ SEQUENCE 540 AA; 59683 MW; 34A3235A29FED5C3 CRC64; MTRKTTQFRN LLNSDRLEFI LEAHNGISAK IVEEAGFKGI WGSGLSLSAQ YGVRDNNEAS WTQVLDMLEF MSDATTIPIL LDGDTGYGNF NNMQRLVRKL EQRDIAAVCI EDKLFPKTNS FIKGTAQPLA DIEEFCGKIK AGKDAQGDDD FSIVARVEAF IAGWGLKEAM RRAEAYRKAG ADAILMHSAL SVPDEILAFK KEWGDRLPVV IVPTKYYATP TDQFREAGIS IAIWANHMIR TAIASMQKNA ATLMAEESLM AIEDSIAPVK EIFRLQGAAE LQEAEKRYLP KRGKAVRAVI LAASRGKELG ELTEKRPKAM VPVSGQPLLA HVVDGYNSVG VKDITVVRGY AKETVNLSNI DYADNDNFES TGELASLSCA LKSLASEDAG KELVVSYGDV LFKKHILQLL LESHADFSIV VDTNWSESVN KGRFADYVQC SRPYGRDAFG QEISLTEMSE HLPEKRTHGE WTGFLKVSSD HRLLLDKLVE SLTAANPDAR MSDLLNALVA NGERVRVIYT TGYWLDIDTL EDVVLAGNLF //