ID D5EI46_CORAD Unreviewed; 743 AA.
AC D5EI46;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 81.
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};
GN Name=murB {ECO:0000256|HAMAP-Rule:MF_00037};
GN OrderedLocusNames=Caka_3073 {ECO:0000313|EMBL:ADE56086.1};
OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS KCTC 12865 / 04OKA010-24).
OC Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC Coraliomargaritaceae; Coraliomargarita.
OX NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE56086.1, ECO:0000313|Proteomes:UP000000925};
RN [1] {ECO:0000313|EMBL:ADE56086.1, ECO:0000313|Proteomes:UP000000925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC {ECO:0000313|Proteomes:UP000000925};
RX PubMed=21304713; DOI=10.4056/sigs.952166;
RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Coraliomargarita akajimensis type strain
RT (04OKA010-24).";
RL Stand. Genomic Sci. 2:290-299(2010).
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|ARBA:ARBA00003921,
CC ECO:0000256|HAMAP-Rule:MF_00037}.
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_00037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00037}.
CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|HAMAP-
CC Rule:MF_00037}.
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DR EMBL; CP001998; ADE56086.1; -; Genomic_DNA.
DR RefSeq; WP_013044802.1; NC_014008.1.
DR AlphaFoldDB; D5EI46; -.
DR STRING; 583355.Caka_3073; -.
DR KEGG; caa:Caka_3073; -.
DR eggNOG; COG0773; Bacteria.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_373732_0_0_0; -.
DR OMA; IINRGHA; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000925; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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: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 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 NCBIfam; TIGR00179; murB; 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};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00037};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00037};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00037};
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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00037};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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_00037}; Reference proteome {ECO:0000313|Proteomes:UP000000925}.
FT DOMAIN 455..622
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 602
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 651
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT ACT_SITE 721
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ SEQUENCE 743 AA; 80622 MW; D7D4185A8C10919F CRC64;
MSPEAGNYLF LGVGGMGMAP LAAWMVQEGY SLAGYDDYMQ EPVRRFLAES GVELLDFVFP
ESLSDYSVVV HSSALQADHP ILQRARELGM TVLRRGEMLA SVASTRRFVA VVGSHGKTTT
TGMIAYGLRE AGIEADYILG GFFNDPAVPA SRHTGSEWLV AEVDESDGTI ESFSPEMTLI
LNVDWDHADR YADAEQLDDA FRGLIQRTVG TVLVPQAADF VERFAADLRE CGQSFSVEPD
SGFNVSNRQA ACAVLERLSG GCCSAVDFSA FPGIARRQGL KLETASSAIY EDYAHHPTEI
AALFASLRKR HPGRRLVVVF QGHRYSRTKQ FKAEFAEVLA EAEECFLLPV YAAHEHPLSG
GTAEDLKEAF GAHVPELLSM DLEGIRRLYA AVSNEACTLA FVGAGDIDQF GAVFTAWSQA
EGREGEAWDR YMAGRVSPDC SLRRDEPLAK KTTMRVGGAA AYYAEPANLC DLRALLKAAQ
LFDLPVFSLG RGSNLIVPDE GYAGLVIRFT AGIWRAVHIL DGQQLWAGAG VRLKEVCGQA
AKAGLAGFEF LEGIPGSLGG SLRMNAGAMG NWMFDVVERV QMLDATGRYL DLPKEAFHFG
YRKVEEISQG IALGAILSSR VAESSESIRE RMDSYSTTRK ASQPRDPSAG CIFKNPDGNY
AGKLIDEHGI KGMSVGAAEV SAVHGNFIVN RGGATATDVI ELVRRVRRAV KERSGYELEP
EVLLLGQQWD ELLKEEDTGD AGA
//