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Database: UniProt
Entry: A0A1A6C3D2_9GAMM
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ID   A0A1A6C3D2_9GAMM        Unreviewed;       305 AA.
AC   A0A1A6C3D2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|ARBA:ARBA00015188, ECO:0000256|HAMAP-Rule:MF_00037};
DE            EC=1.3.1.98 {ECO:0000256|ARBA:ARBA00012518, ECO:0000256|HAMAP-Rule:MF_00037};
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|ARBA:ARBA00031026, ECO:0000256|HAMAP-Rule:MF_00037};
GN   Name=murB {ECO:0000256|HAMAP-Rule:MF_00037};
GN   ORFNames=Thpro_021399 {ECO:0000313|EMBL:OBS09071.1};
OS   Acidihalobacter prosperus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=160660 {ECO:0000313|EMBL:OBS09071.1, ECO:0000313|Proteomes:UP000029273};
RN   [1] {ECO:0000313|EMBL:OBS09071.1, ECO:0000313|Proteomes:UP000029273}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5130 {ECO:0000313|EMBL:OBS09071.1,
RC   ECO:0000313|Proteomes:UP000029273};
RX   PubMed=25342676;
RA   Ossandon F.J., Cardenas J.P., Corbett M., Quatrini R., Holmes D.S.,
RA   Watkin E.;
RT   "Draft Genome Sequence of the Iron-Oxidizing, Acidophilic, and Halotolerant
RT   'Thiobacillus prosperus' Type Strain DSM 5130.";
RL   Genome Announc. 2:0-0(2014).
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|ARBA:ARBA00010485,
CC       ECO:0000256|HAMAP-Rule:MF_00037}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS09071.1}.
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DR   EMBL; JQSG02000003; OBS09071.1; -; Genomic_DNA.
DR   RefSeq; WP_038088942.1; NZ_JQSG02000003.1.
DR   AlphaFoldDB; A0A1A6C3D2; -.
DR   STRING; 160660.BJI67_13360; -.
DR   OrthoDB; 9804753at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000029273; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.90.78.10; 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   3: Inferred from homology;
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};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00037};
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:UP000029273}.
FT   DOMAIN          28..207
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        224
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00037"
SQ   SEQUENCE   305 AA;  32365 MW;  B19AAE0729603882 CRC64;
     MIAAARHREL RGELTHDAPL APLTSWRAGG HADRLYRPAD LEDLREFLRG LSDDEPVLWL
     GLGSNLLVRD GGVRGTVIAT HARLDGLECV GEAGVRAGAG VPGAKLARFA ARAGLVGAEF
     FAGIPGTVGG ALAMNAGAFG GETWRVVRRA QTIERSGNVE WFDVDAFETG YRHVAARDAG
     ERWFVAAEFG FAAGGDPQEL HRRTRDLLAN RAHSQPTGVA SCGSVFRNPP GDYAGRLIEA
     AGLKGLRCGG AQVSEKHGNF ILNTGAATAA DIETLMTTVQ ERVAQQTGIR LVPEVRIVGK
     AEVRT
//
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