ID E9L1F5_9ZZZZ Unreviewed; 447 AA. AC E9L1F5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 22-FEB-2023, entry version 33. DE RecName: Full=UDP-MurNAc-pentapeptide synthetase {ECO:0000256|ARBA:ARBA00031461}; GN ORFNames=CA37-11 {ECO:0000313|EMBL:ADU56034.1}; OS uncultured organism CA37. OC unclassified sequences; environmental samples. OX NCBI_TaxID=941420 {ECO:0000313|EMBL:ADU56034.1}; RN [1] {ECO:0000313|EMBL:ADU56034.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=20945895; DOI=10.1021/ja105825a; RA Banik J.J., Craig J.W., Calle P.Y., Brady S.F.; RT "Tailoring enzyme-rich environmental DNA clones: a source of enzymes for RT generating libraries of unnatural natural products."; RL J. Am. Chem. Soc. 132:15661-15670(2010). 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; HM486074; ADU56034.1; -; Genomic_DNA. DR AlphaFoldDB; E9L1F5; -. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:InterPro. 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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1. DR HAMAP; MF_02019; MurF; 1. 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; IPR035911; MurE/MurF_N. DR InterPro; IPR005863; UDP-N-AcMur_synth. DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1. DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1. DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1. DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1. DR TIGRFAMs; TIGR01143; murF; 1. PE 3: Inferred from homology; FT DOMAIN 31..81 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 108..293 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 317..393 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" SQ SEQUENCE 447 AA; 45305 MW; 14C4C09420C74971 CRC64; MIPLSLDEIA AVVSGTVEGD GAVTVTAPAV LDGRQAEPGG LFVAFAGEHV DGHDYAGQAG RAGAVAVLGS RPTTLPTVVV EDARAALQAL AAHVVARLRD RLTVVGLTGS QGKTSTKDLL AAVLSHTGST VATIGSLNNE LGVPLTMLRT TPDTRFLVLE MGARGIGHIA ELTALVALDV AVVLNVGQAH IGEFGSREAI ATAKAELLQG LVPGGTAILN ADDPRVLVMR ALTDGPALTF GRAEHAHVRV LDLALDRLGR PAFTLRTADA SAPVALPLVG AHQALNASAA AAAGLAAGIP LDVTAATLAT ASLSKWRMEL RGLSGGVSLL NDSYNANPDS TRAALDALAA IEAGRRIAVL GEMRELGDDS EAEHRAIGEY AARAADLVVA VGEAAAPIAE GAGDRAVALA DNDAAVDWLR RALTAGDVVL VKASRLARLD EVAAALA //