(data stored in ACNUC7421 zone)

HOGENOM: AZOC5_1_PE101

ID   AZOC5_1_PE101                        STANDARD;      PRT;   536 AA.
AC   AZOC5_1_PE101; A8IGK6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase; EC=6.3.2
DE   9; (AZOC5_1.PE101).
GN   OrderedLocusNames=AZC_0101;
OS   AZORHIZOBIUM CAULINODANS ORS 571.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AZOC5_1.PE101.
CC       Azorhizobium caulinodans ORS 571, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A8IGK6_AZOC5
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanine +
CC       glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
CC   -!- GENE_FAMILY: HOG000049428 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8IGK6; -.
DR   EMBL; AP009384; BAF86099.1; -; Genomic_DNA.
DR   RefSeq; YP_001523017.1; NC_009937.1.
DR   ProteinModelPortal; A8IGK6; -.
DR   STRING; A8IGK6; -.
DR   GeneID; 5691894; -.
DR   GenomeReviews; AP009384_GR; AZC_0101.
DR   KEGG; azc:AZC_0101; -.
DR   OMA; LERHKTL; -.
DR   ProtClustDB; PRK01390; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00639; MurD; 1; -.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23135:SF2; PTHR23135:SF2; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; Mur_ligase_C; 1.
DR   SUPFAM; SSF53623; Mur_ligase_cen; 1.
DR   TIGRFAMs; TIGR01087; MurD; 1.
DR   HOGENOMDNA; AZOC5_1.PE101; -.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
SQ   SEQUENCE   536 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSRQREMPRF CCACQMRRRS GRRLRHPANS TAARKTVFSR PLRTVARAPL HHDTHRRRIP
     RGAVSFRMFG VMIPVSTFKD RRVAVFGLGG SGLATAQALL AGGAEVIGWD DGEAGRKKAE
     AAGITVSDLH EADWSGFAAL VLAPGVPLTH PTPHWTVGLA QAAGVEIIGD IELFCRERRA
     LKPTAPFAAI TGTNGKSTTT ALLSHLMKVG GRDVQMGGNI GTAILSLEPF KAGRVHVVEC
     SSYQIDLAPG LDPSVGIHLN LTPDHIDRHG TFEHYGAVKE RLIAGVQPGG TAVVGVDDAP
     SAAIADRAEA AGIHVVRISV KQPLADGIWL DGETLVVSEK GAEVFRLPLT GIGSLRGAHN
     AQNAAAAMAA ARGLGLAYEV IAVGMQRFPG LAHRMEQVGT RGKVLFVNDS KATNADAAER
     ALASFSDVFW IAGGKPKAGG ITPLKPFFPR VRKAYLIGEA AADFAATLGD VPHEVVGTLD
     RAVAAAARDA AASSLDHPVV LLSPACASFD QYPNFEVRGD AFRHLVEELP QETAPA
//

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