ID   AP4A_MYCTO              Reviewed;         195 AA.
AC   P9WMK8; L0TA61; O06201; Q7D6W5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=AP-4-A phosphorylase;
DE            EC=2.7.7.53;
DE   AltName: Full=ATP adenylyltransferase;
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase;
DE            Short=AP,A phosphorylase;
GN   OrderedLocusNames=MT2688;
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).
CC   -!- FUNCTION: Catabolizes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A)
CC       into ADP and ATP. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + ATP + H(+) = P(1),P(4)-bis(5'-adenosyl) tetraphosphate +
CC         phosphate; Xref=Rhea:RHEA:16577, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58141,
CC         ChEBI:CHEBI:456216; EC=2.7.7.53;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 divalent metal ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
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DR   EMBL; AE000516; AAK47004.1; -; Genomic_DNA.
DR   PIR; D70571; D70571.
DR   RefSeq; WP_003413484.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMK8; -.
DR   SMR; P9WMK8; -.
DR   EnsemblBacteria; AAK47004; AAK47004; MT2688.
DR   GeneID; 45426616; -.
DR   KEGG; mtc:MT2688; -.
DR   PATRIC; fig|83331.31.peg.2898; -.
DR   HOGENOM; CLU_056776_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0003877; F:ATP adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd01275; FHIT; 1.
DR   Gene3D; 3.30.428.10; -; 1.
DR   InterPro; IPR039383; FHIT.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   Pfam; PF01230; HIT; 1.
DR   SUPFAM; SSF54197; SSF54197; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..195
FT                   /note="AP-4-A phosphorylase"
FT                   /id="PRO_0000427286"
FT   DOMAIN          57..166
FT                   /note="HIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           151..155
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        153
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   195 AA;  21869 MW;  36516FCE8B05D77B CRC64;
     MSDEDRTDRA TEDHTIFDRG VGQRDQLQRL WTPYRMNYLA EAPVKRDPNS SASPAQPFTE
     IPQLSDEEGL VVARGKLVYA VLNLYPYNPG HLMVVPYRRV SELEDLTDLE SAELMAFTQK
     AIRVIKNVSR PHGFNVGLNL GTSAGGSLAE HLHVHVVPRW GGDANFITII GGSKVIPQLL
     RDTRRLLATE WARQP