MTNU_BACSU
ID MTNU_BACSU Reviewed; 259 AA.
AC O31664;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=2-oxoglutaramate amidase {ECO:0000305};
DE EC=3.5.1.111 {ECO:0000305|PubMed:24837359};
GN Name=mtnU {ECO:0000303|PubMed:12022921}; Synonyms=ykrU;
GN OrderedLocusNames=BSU13570;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12022921; DOI=10.1186/1471-2180-2-8;
RA Sekowska A., Danchin A.;
RT "The methionine salvage pathway in Bacillus subtilis.";
RL BMC Microbiol. 2:8-8(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24837359; DOI=10.1016/j.phytochem.2014.04.012;
RA Ellens K.W., Richardson L.G., Frelin O., Collins J., Ribeiro C.L.,
RA Hsieh Y.F., Mullen R.T., Hanson A.D.;
RT "Evidence that glutamine transaminase and omega-amidase potentially act in
RT tandem to close the methionine salvage cycle in bacteria and plants.";
RL Phytochemistry 113:160-169(2015).
CC -!- FUNCTION: Involved in the methylthioribose (MTR) recycling pathway
CC (PubMed:12022921, PubMed:24837359). Probably catalyzes the conversion
CC of 2-oxoglutaramate to 2-oxoglutarate (PubMed:24837359).
CC {ECO:0000269|PubMed:12022921, ECO:0000269|PubMed:24837359}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutaramate + H2O = 2-oxoglutarate + NH4(+);
CC Xref=Rhea:RHEA:32963, ChEBI:CHEBI:15377, ChEBI:CHEBI:16769,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938; EC=3.5.1.111;
CC Evidence={ECO:0000305|PubMed:24837359};
CC -!- DISRUPTION PHENOTYPE: Impaired growth on methylthioribose (MTR) as sole
CC sulfur source. {ECO:0000269|PubMed:12022921,
CC ECO:0000269|PubMed:24837359}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13230.1; -; Genomic_DNA.
DR PIR; E69863; E69863.
DR RefSeq; NP_389240.1; NC_000964.3.
DR RefSeq; WP_003232495.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31664; -.
DR SMR; O31664; -.
DR STRING; 224308.BSU13570; -.
DR PaxDb; O31664; -.
DR PRIDE; O31664; -.
DR EnsemblBacteria; CAB13230; CAB13230; BSU_13570.
DR GeneID; 939328; -.
DR KEGG; bsu:BSU13570; -.
DR PATRIC; fig|224308.179.peg.1474; -.
DR eggNOG; COG0388; Bacteria.
DR InParanoid; O31664; -.
DR OMA; GNTYRES; -.
DR PhylomeDB; O31664; -.
DR BioCyc; BSUB:BSU13570-MON; -.
DR BioCyc; MetaCyc:BSU13570-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0106008; F:2-oxoglutaramate amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..259
FT /note="2-oxoglutaramate amidase"
FT /id="PRO_0000360754"
FT DOMAIN 3..238
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 259 AA; 29399 MW; 89A2233252CCBCFA CRC64;
MKWTISCLQF DISYGKPSEN IKKAEFFIEK ESKHADVLVL PELWTTGYDL ANLDELADED
GRSAQSWLKK TAKKHGVHIV AGSVAVRKNS DVYNTMYIAD KEGQIIKEYR KAHLFQLMDE
HLYLSAGSED GYFELDGVKS SGLICYDIRF PEWIRKHTTK GANVLFISAE WPLPRLDHWK
SLLIARAIEN QCFVAACNCT GSNPDNEFAG HSLIIDPWGR VLAEGGREEG IVRAEIDLQE
SAEVRESIPV FDDIRKDLY
