NAGA_BACSU
ID NAGA_BACSU Reviewed; 396 AA.
AC O34450;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:14557261};
DE Short=GlcNAc 6-P deacetylase {ECO:0000303|PubMed:14557261};
DE EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18};
GN Name=nagA; OrderedLocusNames=BSU35010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION.
RX PubMed=21602348; DOI=10.1128/jb.00264-11;
RA Bertram R., Rigali S., Wood N., Lulko A.T., Kuipers O.P., Titgemeyer F.;
RT "Regulon of the N-acetylglucosamine utilization regulator NagR in Bacillus
RT subtilis.";
RL J. Bacteriol. 193:3525-3536(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH IRON AND REACTION
RP PRODUCT, FUNCTION, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=168 / IG20;
RX PubMed=14557261; DOI=10.1074/jbc.m310165200;
RA Vincent F., Yates D., Garman E., Davies G.J., Brannigan J.A.;
RT "The three-dimensional structure of the N-acetylglucosamine-6-phosphate
RT deacetylase, NagA, from Bacillus subtilis: a member of the urease
RT superfamily.";
RL J. Biol. Chem. 279:2809-2816(2004).
CC -!- FUNCTION: Involved in the first committed step in the biosynthesis of
CC amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group
CC of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-
CC phosphate and acetate. {ECO:0000269|PubMed:14557261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25;
CC Evidence={ECO:0000269|PubMed:14557261};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:14557261};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000269|PubMed:14557261};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 4/5. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14557261}.
CC -!- INDUCTION: Expression is repressed by the HTH-type transcriptional
CC regulator NagR. {ECO:0000269|PubMed:21602348}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000305}.
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DR EMBL; AF017113; AAC67285.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15506.1; -; Genomic_DNA.
DR PIR; A69664; A69664.
DR RefSeq; NP_391381.1; NC_000964.3.
DR RefSeq; WP_003243413.1; NZ_JNCM01000033.1.
DR PDB; 2VHL; X-ray; 2.05 A; A/B=1-396.
DR PDBsum; 2VHL; -.
DR AlphaFoldDB; O34450; -.
DR SMR; O34450; -.
DR STRING; 224308.BSU35010; -.
DR DrugBank; DB02657; Glucosamine 6-Phosphate.
DR MEROPS; M38.983; -.
DR jPOST; O34450; -.
DR PaxDb; O34450; -.
DR EnsemblBacteria; CAB15506; CAB15506; BSU_35010.
DR GeneID; 936621; -.
DR KEGG; bsu:BSU35010; -.
DR PATRIC; fig|224308.179.peg.3789; -.
DR eggNOG; COG1820; Bacteria.
DR InParanoid; O34450; -.
DR OMA; HAFNAMP; -.
DR PhylomeDB; O34450; -.
DR BioCyc; BSUB:BSU35010-MON; -.
DR SABIO-RK; O34450; -.
DR UniPathway; UPA00629; UER00683.
DR EvolutionaryTrace; O34450; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IDA:UniProtKB.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113:SF14; PTHR11113:SF14; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00221; nagA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Iron; Metal-binding;
KW Reference proteome.
FT CHAIN 1..396
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000170914"
FT ACT_SITE 281
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:14557261"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 65
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 147..148
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 226..227
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 255..258
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14557261"
FT BINDING 314..316
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14557261"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:2VHL"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:2VHL"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:2VHL"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:2VHL"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:2VHL"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2VHL"
SQ SEQUENCE 396 AA; 42622 MW; 852D53C71BAD6F54 CRC64;
MAESLLIKDI AIVTENEVIK NGYVGINDGK ISTVSTERPK EPYSKEIQAP ADSVLLPGMI
DIHIHGGYGA DTMDASFSTL DIMSSRLPEE GTTSFLATTI TQEHGNISQA LVNAREWKAA
EESSLLGAEL LGIHLEGPFV SPKRAGAQPK EWIRPSDVEL FKKWQQEAGG LIKIVTLAPE
EDQHFELIRH LKDESIIASM GHTDADSALL SDAAKAGASH MTHLYNAMSP FHHREPGVIG
TALAHDGFVT ELIADGIHSH PLAAKLAFLA KGSSKLILIT DSMRAKGLKD GVYEFGGQSV
TVRGRTALLS DGTLAGSILK MNEGARHMRE FTNCSWTDIA NITSENAAKQ LGIFDRKGSV
TVGKDADLVI VSSDCEVILT ICRGNIAFIS KEADQI
