ID   Y0571_MYCTO             Reviewed;         443 AA.
AC   P9WHK0; L0T5R8; O53768; Q7D9M2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Putative phosphoribosyl transferase MT0597;
GN   OrderedLocusNames=MT0597;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12953092; DOI=10.1084/jem.20030205;
RA   Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA   Sherman D.R., Schoolnik G.K.;
RT   "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT   tuberculosis dormancy program.";
RL   J. Exp. Med. 198:705-713(2003).
CC   -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC       reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC       {ECO:0000269|PubMed:12953092}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the dienelactone
CC       hydrolase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44820.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44820.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70933; B70933.
DR   RefSeq; WP_003403001.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHK0; -.
DR   SMR; P9WHK0; -.
DR   ESTHER; myctu-y0571; DLH-S.
DR   PRIDE; P9WHK0; -.
DR   EnsemblBacteria; AAK44820; AAK44820; MT0597.
DR   KEGG; mtc:MT0597; -.
DR   PATRIC; fig|83331.31.peg.629; -.
DR   HOGENOM; CLU_050038_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF01738; DLH; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..443
FT                   /note="Putative phosphoribosyl transferase MT0597"
FT                   /id="PRO_0000428171"
SQ   SEQUENCE   443 AA;  46655 MW;  CC64EF0CE8C598A8 CRC64;
     MKLFDDRGDA GRQLAQRLAQ LSGKAVVVLG LPRGGVPVAF EVAKSLQAPL DVLVVRKLGV
     PFQPELAFGA IGEDGVRVLN DDVVRGTHLD AAAMDAVERK QLIELQRRAE RFRRGRDRIP
     LTGRIAVIVD DGIATGATAK AACQVARAHG ADKVVLAVPI GPDDIVARFA GYADEVVCLA
     TPALFFAVGQ GYRNFTQTSD DEVVAFLDRA HRDFAEAGAI DAAADPPLRD EEVQVVAGPV
     PVAGHLTVPE KPRGIVVFAH GSGSSRHSIR NRYVAEVLTG AGFATLLFDL LTPEEERNRA
     NVFDIELLAS RLIDVTGWLA TQPDTASLPV GYFGASTGAG AALVAAADPR VNVRAVVSRG
     GRPDLAGDSL GSVVAPTLLI VGGRDQVVLE LNQRAQAVIP GKCQLTVVPG ATHLFEEPGT
     LEQVAKLACD WFIDHLCGPG PSG