YHCX_BACSU
ID YHCX_BACSU Reviewed; 513 AA.
AC P54608;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Hydrolase YhcX;
DE EC=3.5.-.-;
GN Name=yhcX; OrderedLocusNames=BSU09250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969498; DOI=10.1099/13500872-142-11-3021;
RA Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RT "A 22 kb DNA sequence in the cspB-glpPFKD region at 75 degrees on the
RT Bacillus subtilis chromosome.";
RL Microbiology 142:3021-3026(1996).
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 SEQUENCE REVISION TO 137.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000305}.
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DR EMBL; X96983; CAA65708.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12753.2; -; Genomic_DNA.
DR PIR; D69824; D69824.
DR RefSeq; NP_388806.2; NC_000964.3.
DR RefSeq; WP_003245514.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P54608; -.
DR SMR; P54608; -.
DR STRING; 224308.BSU09250; -.
DR jPOST; P54608; -.
DR PaxDb; P54608; -.
DR PRIDE; P54608; -.
DR EnsemblBacteria; CAB12753; CAB12753; BSU_09250.
DR GeneID; 939265; -.
DR KEGG; bsu:BSU09250; -.
DR PATRIC; fig|224308.179.peg.997; -.
DR eggNOG; COG0388; Bacteria.
DR eggNOG; COG3153; Bacteria.
DR InParanoid; P54608; -.
DR OMA; GLIQWQM; -.
DR PhylomeDB; P54608; -.
DR BioCyc; BSUB:BSU09250-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR001110; UPF0012_CS.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..513
FT /note="Hydrolase YhcX"
FT /id="PRO_0000213260"
FT DOMAIN 14..212
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 229..484
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 345
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 379
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT CONFLICT 137
FT /note="N -> S (in Ref. 1; CAA65708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 60218 MW; 6462F5AA4B67AAD4 CRC64;
MSEKLDLTRF EKKMVIRNIE EKDIDKIIDL QKDCFPGMEP WKREHLISHL EHFPEGQFCA
EFEGEIIGSC SSLLINFDEY DDRHTWQDIT DDGYITNHNP DGLNMYGIEV MVHPKYRRMK
IGHRLYEARK DLARRLNLKS IIIGGRIPNY HKYAEEMTAR EYVEQVTRHQ IYDPVLSFQL
MNGFTLMRIN PNYLPDDTAS IKYATLMEWN NVDYLPQQTK RYYKSAFPVR ICVIQYEMKK
IYSFEEFANQ VEYYVDVASD ARSDFAVFPE IFTTQLMSFL EERSPSLAVQ RITEYTEDYI
SLFTDLAVKY NVNIIGGSHF VEEEGKIYNI AYLFRRDGTI EKQYKLHITP NERKWWGISA
GDQVRVFDTD CGKIAIQICY DIEFPELARI AADKGAKIIF TPFCTEDRQG YLRVRYCSQA
RAVENQIYTV ISGTVGNLPQ TENMDIQYAQ SGIFAPSDFE FARDGIVGET NPNIEMVVIG
DVDLEILRRQ RQNGTVRQLK DRRRDIYHIQ YKK