ID MURB_VIBCH Reviewed; 347 AA.
AC Q9KV40;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000255|HAMAP-Rule:MF_00037};
DE EC=1.3.1.98 {ECO:0000255|HAMAP-Rule:MF_00037};
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00037};
GN Name=murB {ECO:0000255|HAMAP-Rule:MF_00037}; OrderedLocusNames=VC_0318;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Cell wall formation. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00037};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00037};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00037}.
CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000255|HAMAP-
CC Rule:MF_00037}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93491.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93491.1; ALT_INIT; Genomic_DNA.
DR PIR; D82337; D82337.
DR RefSeq; NP_229972.1; NC_002505.1.
DR PDB; 3I99; X-ray; 2.20 A; A=1-347.
DR PDBsum; 3I99; -.
DR AlphaFoldDB; Q9KV40; -.
DR SMR; Q9KV40; -.
DR STRING; 243277.VC_0318; -.
DR DNASU; 2615109; -.
DR EnsemblBacteria; AAF93491; AAF93491; VC_0318.
DR KEGG; vch:VC_0318; -.
DR PATRIC; fig|243277.26.peg.295; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_0_0_6; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q9KV40; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; 3.90.78.10; 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; 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; PTHR21071; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1.
DR PANTHER; PTHR21071:SF4; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF02873; MurB_C; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF56194; Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..347
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179285"
FT DOMAIN 17..187
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 327
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3I99"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3I99"
FT TURN 121..125
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:3I99"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3I99"
FT TURN 169..174
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 175..187
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:3I99"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3I99"
FT HELIX 302..320
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:3I99"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:3I99"
SQ SEQUENCE 347 AA; 38271 MW; C4758B7E14A31CD6 CRC64;
MQIQLGANLK PYHTFGIEQL AAQLVVAESI DDLKALYCSA EWASLPKLII GKGSNMLFTC
HYTGMIVVNR LNGIEHQQDD DYHRLHVAGG EDWPSLVSWC VEQGIGGLEN LALIPGCAGS
APIQNIGAYG VEFKDVCDYV EYLCLETGTV KRLTMEECQF GYRDSIFKHQ LYQKAVVTAV
GLKFAKAWQP IIQYGPLKDL SSDCAIHDVY QRVCATRMEK LPDPAVMGNA GSFFKNPVIS
QQAFARLQIE HPDVVAYPAE QGVKVAAGWL IDQAGLKGHQ IGGAKVHPKQ ALVIVNTGDA
SAQDVLMLAA DIQQRVFNCY GIELEHEVRF IGESEETNLK QWMSEQA
//
