ID A0A0G0USN4_9BACT Unreviewed; 771 AA. AC A0A0G0USN4; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 27-MAR-2024, entry version 45. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00046, ECO:0000256|HAMAP-Rule:MF_01963}; DE Includes: DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00046}; DE EC=6.3.2.8 {ECO:0000256|HAMAP-Rule:MF_00046}; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046}; DE Includes: DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963}; DE Short=PNP {ECO:0000256|HAMAP-Rule:MF_01963}; DE EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01963}; GN Name=murC {ECO:0000256|HAMAP-Rule:MF_00046}; GN ORFNames=UU43_C0002G0042 {ECO:0000313|EMBL:KKR91733.1}; OS Candidatus Falkowbacteria bacterium GW2011_GWA2_41_14. OC Bacteria; Candidatus Falkowbacteria. OX NCBI_TaxID=1618635 {ECO:0000313|EMBL:KKR91733.1, ECO:0000313|Proteomes:UP000034190}; RN [1] {ECO:0000313|EMBL:KKR91733.1, ECO:0000313|Proteomes:UP000034190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large RT radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- FUNCTION: Purine nucleoside phosphorylase involved in purine salvage. CC {ECO:0000256|HAMAP-Rule:MF_01963}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; CC Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, CC ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; CC Evidence={ECO:0000256|ARBA:ARBA00001677, ECO:0000256|HAMAP- CC Rule:MF_00046}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + CC alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01963}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC {ECO:0000256|HAMAP-Rule:MF_01963}. CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000256|HAMAP- CC Rule:MF_01963}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046}. CC -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA CC phosphorylases based on sequence homology, it lacks several conserved CC amino acids in the substrate binding pocket that confer specificity CC towards MTA. {ECO:0000256|HAMAP-Rule:MF_01963}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP- CC Rule:MF_00046}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01963}. 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:KKR91733.1}. 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; LCAP01000002; KKR91733.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G0USN4; -. DR PATRIC; fig|1618635.3.peg.202; -. DR UniPathway; UPA00219; -. DR UniPathway; UPA00606; -. DR Proteomes; UP000034190; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:InterPro. DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1. DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1. DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1. DR HAMAP; MF_01963; MTAP; 1. DR HAMAP; MF_00046; MurC; 1. DR InterPro; IPR010044; MTAP. DR InterPro; IPR036565; Mur-like_cat_sf. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR036615; Mur_ligase_C_dom_sf. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR035994; Nucleoside_phosphorylase_sf. DR InterPro; IPR018099; Purine_phosphorylase-2_CS. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC. DR NCBIfam; TIGR01694; MTAP; 1. DR NCBIfam; TIGR01082; murC; 1. DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1. DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF51984; MurCD N-terminal domain; 1. DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1. DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00046}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00046}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00046}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00046}; Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963}. FT DOMAIN 12..250 FT /note="Nucleoside phosphorylase" FT /evidence="ECO:0000259|Pfam:PF01048" FT DOMAIN 294..396 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 400..591 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 612..693 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT BINDING 19 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 61..62 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 94..95 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 192 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 215..217 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 402..408 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00046" FT SITE 173 FT /note="Important for substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT SITE 228 FT /note="Important for substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" SQ SEQUENCE 771 AA; 86035 MW; 0B4D3664D4676934 CRC64; MNNNLINMNK IKIAIIGGSG LDDPGILKNA KKVNLATPFG ATAAPLICGQ IDGVDMVVLA RHGINHTFMP TKVPYRANIW ALKEIGCTHI IATTACGSLQ EKIKPRDLIF LDQFIDFTKH RNLTFFEDKV VHTAMADPFC PDLREILIKT AEELKFAHHK QGTIITIEGP RFSTRAESRF FKQMGADVIN MSTVPEVILA REVGICYGSV AMATDYDAWR KDEKAVTWGM VMQVMKDNTN NVVKLLLNII PKIALELADE ECENCGYIRS EKITNCKPPP NRFYIYMDLN KIKKIYLIGI KGVGMTMLAQ YLVGQNIDVS GSDGPEKYMT DAVLKKCGIK IIEKFDAKNI PHDADLIIYS TAYNAETNVE VAVALAGKIK IMTYAQALGE TFNQKYGIAV VGSHGKTTTT AWLGYVMKMS GLGPSVMAGA PVPQFDGCSI SGQADYLVIE ADEYQNKLQY YQPKAVLLNN IDYDHPDFFP TATDYENTYI EFIKKIPAKG FLVANFDDSL IRKIAQVNCR GKVITYAIDE TADYVAFDLK ANNGKQYFKV KLEVEDELDE EETRVEELGG FSIQLAGRHN ILNALAVIAT AIELNIELFK IRKYLAEFTG TARRMQALGE FRGATVIDDY AHHPTEIKAT VSAVRQKYGS RKLMVAFQPH TFSRTKALFN DFVKSFAQVD ELIILDIYGS AREKPGGAHS RDLAEKIRIR NQESLRRQGF GGQAGIRQTV KYISTLAECE RYLRDRVERN DVVVLMGAGD IFRVGENLVK G //