ID M1AN22_SOLTU Unreviewed; 577 AA.
AC M1AN22;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211};
DE EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400026358, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400026358}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400026358};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR AlphaFoldDB; M1AN22; -.
DR STRING; 4113.M1AN22; -.
DR PaxDb; 4113-PGSC0003DMT400026358; -.
DR EnsemblPlants; PGSC0003DMT400026358; PGSC0003DMT400026358; PGSC0003DMG400010168.
DR Gramene; PGSC0003DMT400026358; PGSC0003DMT400026358; PGSC0003DMG400010168.
DR eggNOG; ENOG502QPWX; Eukaryota.
DR InParanoid; M1AN22; -.
DR OMA; ELMRMKY; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1AN22; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00046; MurC; 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; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT DOMAIN 67..169
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 199..398
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 426..508
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 577 AA; 62865 MW; 32962DDE028894F9 CRC64;
MSPANYPERS CSYSQAITLT NRRQIVQSRK LKYARTTSPS LKLSPVITNC DNAEVIGARE
CKGKEWIHFV GVGGCGLSAL AMLALKQGYE VSGSDMMWSD AMDALREAGA RVYVGHSELN
LRKNNGLVPD ALVVSSAIRG GNVEILHAES VGIPVYKRGA WLGRITKGYN LIAVSGSHAF
FNTKISLLVL SVDLFTNAGK TTSASMLAYV LNAMGGDLTA VIGARVPQLA ERNIICGTGC
NFVLEADEYD CCFLGVTPQI AVVTNVDWEH VDMFQDEVDY HQIVSISSQE AVKTIFRKFI
GQIRVGGHLI LCGDSPGAYS LVNKTGSGSA LPVLHNDAFQ ISTYGISSCN DWHALSISPN
SCGGSDYQLF HKGLHIADIS LQMPGVHNVL NSLAVIATIS ALSTDQKNFL SSIASLKLHL
QNFEGVSRRF ERIGTVRGCH IYDDYAHHPT EIQAVLQAAR QRFPFQKLVV IFQPHTYSRL
AALKDDFAIA FTNADRVVIT EIYEARETNL WKINGRDLAI SIVDPPSEFI PSLIQVLEML
VVHISKDPDH ETVILTLGAE KLTILGTDPV NDTEGVV
//
