UniProt: A0A0P0G3U2

Database: UniProt
Entry: A0A0P0G3U2_9BACT

LinkDB:  A0A0P0G3U2_9BACT 
Original site:  A0A0P0G3U2_9BACT

All links

Ontology (10)   
   GO (10)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (14)   
   Pfam (5)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (36)   

Download RDF

ID   A0A0P0G3U2_9BACT        Unreviewed;       766 AA.
AC   A0A0P0G3U2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|HAMAP-Rule:MF_00046};
DE   Includes:
DE     RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|HAMAP-Rule:MF_00037};
DE              EC=1.3.1.98 {ECO:0000256|HAMAP-Rule:MF_00037};
DE     AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00037};
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};
GN   Name=murC {ECO:0000256|HAMAP-Rule:MF_00046,
GN   ECO:0000313|EMBL:ALJ56536.1};
GN   Synonyms=murB {ECO:0000256|HAMAP-Rule:MF_00037};
GN   ORFNames=AMD24_00355 {ECO:0000313|EMBL:ALJ56536.1};
OS   Candidatus Xiphinematobacter sp. Idaho Grape.
OC   Bacteria; Verrucomicrobiota; Spartobacteria; Xiphinematobacter.
OX   NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56536.1, ECO:0000313|Proteomes:UP000062177};
RN   [1] {ECO:0000313|EMBL:ALJ56536.1, ECO:0000313|Proteomes:UP000062177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56536.1,
RC   ECO:0000313|Proteomes:UP000062177};
RX   PubMed=26362082; DOI=10.1093/gbe/evv176;
RA   Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT   "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont Suggest a
RT   Role in Nutritional Symbiosis.";
RL   Genome Biol. Evol. 7:2727-2746(2015).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|ARBA:ARBA00003921,
CC       ECO:0000256|HAMAP-Rule:MF_00046}.
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=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-
CC         N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98;
CC         Evidence={ECO:0000256|ARBA:ARBA00001501, ECO:0000256|HAMAP-
CC         Rule:MF_00037};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_00037};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00046}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00037}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00046}.
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; CP012665; ALJ56536.1; -; Genomic_DNA.
DR   RefSeq; WP_062100405.1; NZ_CP012665.1.
DR   AlphaFoldDB; A0A0P0G3U2; -.
DR   STRING; 1704307.AMD24_00355; -.
DR   KEGG; xii:AMD24_00355; -.
DR   PATRIC; fig|1704307.3.peg.392; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000062177; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-UniRule.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 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; 3.90.78.10; UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   HAMAP; MF_00037; MurB; 1.
DR   HAMAP; MF_00046; MurC; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
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; IPR003170; MurB.
DR   InterPro; IPR011601; MurB_C.
DR   InterPro; IPR036635; MurB_C_sf.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR   NCBIfam; TIGR00179; murB; 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; PF01565; FAD_binding_4; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   Pfam; PF02873; MurB_C; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 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; SSF56194; Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 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   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00037};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_00037};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00037};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00046};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00037};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00046}; Reference proteome {ECO:0000313|Proteomes:UP000062177}.
FT   DOMAIN          495..660
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        640
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        688
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        758
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   BINDING         123..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   766 AA;  83850 MW;  1095A573C6DA9B08 CRC64;
     MITTSYLASL LLVDVPLRIH LIGVAGSGMS ALAVLLLALG HRVSGSDKVD TLEIRQLTQL
     GLVFETPHRA EHVRGVDLVA QSSAVKPGNV ALDEAIRLGI PIARRADILA AIMTYKRGIL
     VCGMHGKTTT TAMAAHVLRL GGLKPCHYVG ADIPILGANA RWDSESEYFV VEGDESDGSL
     TTYFPEHALV LNVEPEHLDF YQDQDAIDDV FSRLIAQTSG WTFYCADDAG ARRVCTSHPR
     TVCYGTNASC DYWMELFSSS RNGGILTQLA IYHRKSFLGN IQLNVPGRHN ALNALAVTAL
     AMELGVPFDL IAAALRSFRG AKRRFEIKFQ DSLQIIVDDY GHHPTEIQAT LSTARSFGFQ
     RIIVMFQPHR YSRTQALYRQ FGTAFYGADY VLVTDIYPAG EEPIPGISSQ TIVEALQKAG
     HPRVQSHSSI ATIHQQVGRN LLERDLVISL GAGDIYEASN RLAKDLTMRK RLLTAMGPGS
     IRLYEPMSKH TTLRVGGPAQ FWVEPQTEEG FIDLVRLCST ENIPLTVIGR GSNLLVRDGG
     IPGVVVHLGH GQFLQSQPNG HSIVAGAGVR FKQISCMAYR FGIGGFEWME GIPGSLGGGL
     RMNAGAMEVQ LFDQVVCVRC CDQKGNILIK TPPELNVHYR NTPDFACHYV LSATLQGYAS
     SPKEIDHRLR ESKRKRHQSQ PIAASAGCIF KNPREVPAGK LIEELGLKNF SIGKARISEI
     HGNFIVNDGS ASAGEILTLI KEIRTIAKRE RGIELQTEVQ IVGENL
//

DBGET integrated database retrieval system