MURD_THEMA
ID MURD_THEMA Reviewed; 430 AA.
AC Q9WY76;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_00639};
DE EC=6.3.2.9 {ECO:0000255|HAMAP-Rule:MF_00639};
DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00639};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_00639};
GN Name=murD {ECO:0000255|HAMAP-Rule:MF_00639}; OrderedLocusNames=TM_0234;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00639};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC Rule:MF_00639}.
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DR EMBL; AE000512; AAD35325.1; -; Genomic_DNA.
DR PIR; D72402; D72402.
DR RefSeq; NP_228048.1; NC_000853.1.
DR RefSeq; WP_004082930.1; NZ_CP011107.1.
DR PDB; 4BUC; X-ray; 2.17 A; A/B=1-430.
DR PDBsum; 4BUC; -.
DR AlphaFoldDB; Q9WY76; -.
DR SMR; Q9WY76; -.
DR STRING; 243274.THEMA_03555; -.
DR EnsemblBacteria; AAD35325; AAD35325; TM_0234.
DR KEGG; tma:TM0234; -.
DR eggNOG; COG0771; Bacteria.
DR InParanoid; Q9WY76; -.
DR OMA; CNFENYL; -.
DR OrthoDB; 1093223at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate 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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR HAMAP; MF_00639; MurD; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01087; murD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..430
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109113"
FT BINDING 109..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 225..237
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 325..334
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 351..358
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:4BUC"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:4BUC"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:4BUC"
SQ SEQUENCE 430 AA; 49154 MW; 491D71CE4201B2C8 CRC64;
MKIGFLGFGK SNRSLLKYLL NHQEAKFFVS EAKTLDGETK KFLEEHSVEY EEGGHTEKLL
DCDVVYVSPG IKPDTSMIEL LSSRGVKLST ELQFFLDNVD PKKVVGITGT DGKSTATALM
YHVLSGRGFK TFLGGNFGTP AVEALEGEYD YYVLEMSSFQ LFWSERPYLS NFLVLNISED
HLDWHSSFKE YVDSKLKPAF LQTEGDLFVY NKHIERLRNL EGVRSRKIPF WTDENFATEK
ELIVRGKKYT LPGNYPYQMR ENILAVSVLY MEMFNELESF LELLRDFKPL PHRMEYLGQI
DGRHFYNDSK ATSTHAVLGA LSNFDKVVLI MCGIGKKENY SLFVEKASPK LKHLIMFGEI
SKELAPFVGK IPHSIVENME EAFEKAMEVS EKGDVILLSP GGASFDMYEN YAKRGEHFRE
IFKRHGGDEV
