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Database: UniProt/TrEMBL
Entry: D9SJN2_GALCS
LinkDB: D9SJN2_GALCS
Original site: D9SJN2_GALCS 
ID   D9SJN2_GALCS            Unreviewed;       631 AA.
AC   D9SJN2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-SEP-2017, entry version 61.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|HAMAP-Rule:MF_00047};
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=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE              EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
DE     AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE     AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=murB {ECO:0000256|HAMAP-Rule:MF_00037};
GN   Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=Galf_0337 {ECO:0000313|EMBL:ADL54381.1};
OS   Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS   capsiferriformans (strain ES-2)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL54381.1, ECO:0000313|Proteomes:UP000001235};
RN   [1] {ECO:0000313|EMBL:ADL54381.1, ECO:0000313|Proteomes:UP000001235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-2 {ECO:0000313|EMBL:ADL54381.1,
RC   ECO:0000313|Proteomes:UP000001235};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N.,
RA   Ivanova N., Mikhailova N., Shelobolina E.S., Picardal F., Roden E.,
RA   Emerson D., Woyke T.;
RT   "Complete sequence of Gallionella capsiferriformans ES-2.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754456}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00754451}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-
CC       N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH.
CC       {ECO:0000256|HAMAP-Rule:MF_00037}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00037};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00754472};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00754454};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00754475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00644812}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00037}.
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DR   EMBL; CP002159; ADL54381.1; -; Genomic_DNA.
DR   ProteinModelPortal; D9SJN2; -.
DR   STRING; 395494.Galf_0337; -.
DR   EnsemblBacteria; ADL54381; ADL54381; Galf_0337.
DR   KEGG; gca:Galf_0337; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG0812; LUCA.
DR   eggNOG; COG1181; LUCA.
DR   OMA; ILPARIH; -.
DR   OrthoDB; POG091H00GT; -.
DR   BioCyc; GCAP395494:GHXI-349-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001235; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.90.78.10; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   HAMAP; MF_00037; MurB; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR003170; MurB.
DR   InterPro; IPR011601; MurB_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF02873; MurB_C; 1.
DR   TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
DR   TIGRFAMs; TIGR00179; murB; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644673};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00037};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00037};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001235};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00754427};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00037};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00037};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:ADL54381.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00754439};
KW   Manganese {ECO:0000256|SAAS:SAAS00754447};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00754442};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00037};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00037,
KW   ECO:0000313|EMBL:ADL54381.1};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001235}.
FT   DOMAIN       32    200       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
FT   DOMAIN      431    626       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   ACT_SITE    176    176       {ECO:0000256|HAMAP-Rule:MF_00037}.
FT   ACT_SITE    229    229       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00037}.
FT   ACT_SITE    299    299       {ECO:0000256|HAMAP-Rule:MF_00037}.
SQ   SEQUENCE   631 AA;  67539 MW;  40B7AFF1A6D13D42 CRC64;
     MNMSEPGQFI AAVLRGKLSL DQSMRRHTSW RVGGAADRVY QPADLDDLRV YLCSLPLDEP
     LVAVGLGSNL LVRDGGVRGT VLLMHGALTE LAMQQDGLIY VQAGVPGAKL ARFAANHDLA
     GAEFCAGIPG TLGGMLAMNA GCYGSEIWQH VVRVQVVTRS GELIERASSE YQIAYRSVTK
     KQDGASDEFF VGAWLSFVQG DGQVARQNIK ELLAKRISSQ PLNLPNAGSV FRNPANDYAA
     RLIEQCGLKG KKIGGAQVSE KHANFIVNVD NATADEIENL ICQVRQTVMT QTGVDLHPEV
     KIIGEASVKM ANSKTDFKTL NPEFSTLNPA AYGKVAVLFG GRSAEREVSL KSGAAVLASL
     LRSGVDAHAF DPASRSLQEL QEQGFDRVFI ALHGRFGEDG TVQGALELLG IPYTGSGVMA
     SSLGMDKWRS KLVWQAGGLP VPDFMMLAEQ SEPLDVIGKL GLPLFVKPAN EGSSVGISKV
     KAVGELQAAY REAARHDPLV IAERFIGGGE YTVAILGDQV LPVIKIEPAN EFYDFEAKYL
     RDDTCYRCPS GLDAASEAKM QGLAQAAFAL IGGQGWGRVD FLMSEAGQPY VLEANTSPGM
     TDHSLVPMAA RQAGISFDEL VLRVLGMAHV G
//
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