UniProt: B2UPW2

Database: UniProt
Entry: B2UPW2_AKKM8

LinkDB:  B2UPW2_AKKM8 
Original site:  B2UPW2_AKKM8

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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)   

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ID   B2UPW2_AKKM8            Unreviewed;       765 AA.
AC   B2UPW2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=murB {ECO:0000256|HAMAP-Rule:MF_00037};
GN   Synonyms=murC {ECO:0000256|HAMAP-Rule:MF_00046};
GN   OrderedLocusNames=Amuc_0660 {ECO:0000313|EMBL:ACD04497.1};
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD04497.1, ECO:0000313|Proteomes:UP000001031};
RN   [1] {ECO:0000313|Proteomes:UP000001031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC   / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
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}.
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DR   EMBL; CP001071; ACD04497.1; -; Genomic_DNA.
DR   RefSeq; WP_012419712.1; NZ_CP071807.1.
DR   AlphaFoldDB; B2UPW2; -.
DR   STRING; 349741.Amuc_0660; -.
DR   PaxDb; 349741-Amuc_0660; -.
DR   KEGG; amu:Amuc_0660; -.
DR   eggNOG; COG0773; Bacteria.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_373732_0_0_0; -.
DR   OrthoDB; 9804126at2; -.
DR   BioCyc; AMUC349741:G1GBX-718-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001031; 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:UP000001031}.
FT   DOMAIN          491..656
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        636
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        684
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        754
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   BINDING         122..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   765 AA;  83165 MW;  F89A8CA096214461 CRC64;
     MIETLRKRLT DREHPARLHL IGVAGSGMSG LALMLMEMGH RVSGCDRVTS AETERLQSLG
     LSFSCPHSAD AVSDAEIVIY SSAIRADNPA LAAARKLNIP CMRRAECLAA ILNGKKGVVV
     SGTHGKTTTS ALCAHLMREG RMRPCHYVGA EIPVLGTNAH WNEDSEYLVA EGDESDGTLV
     NYIPEHSIVL NIEPEHLDHY KDLDEIKAVF DRLCSQTRGK IIYCRAHPGA EDVCAKYPNS
     VSYGWSDADY TATDVLERRG RTLFTVLKGK EELGRVELGI PGRHNVLNSL AAIALATELG
     VDFPAVTRGL ASFAGAKRRF ETKYLSSSIR IVDDYGHHPT EIAATLQTAR SLQPNRLVVY
     FQPHRYTRTQ LLADDFGKVL QEADLVFVAD VYPASELPIE GVSGQTIINA MHRHGPVETR
     YLPDLGIAHH TIGNALKPGD LFLTLGAGNV HECGMRIARD LALLEDLERT AGGSLEGKLY
     EPMSRHTTMG VGGCAQYWLE PSTFSGMQAA VNYCRDRNIP VHVIGRGSNI IVRDGGLRGA
     VIHPSGGEFD VLEIQGNRLT AGAGVRLKKL VSTAVQNGLG GLEWMDGIPG NVGGSLRMNA
     GAMGMDMVKN LVSVTCLDED GEIRSHTREE LNAQYRSIPD LVHNFVLQAV FEAQPAPAEE
     MERLLEAARA RRKLSQPVGA SAGCIFKNPP EIPAGRLIDE LGLKGACVGD ACVSDVHANF
     IINRGHARAR DITILIDMIR KEAKENRGID LKSEAQVIGD RDPQF
//

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