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PHS_MYCTO
ID   PHS_MYCTO               Reviewed;          94 AA.
AC   P9WI92; L0T7H1; P0A5S2; P58241;
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 pterin-4-alpha-carbinolamine dehydratase;
DE            Short=PHS;
DE            EC=4.2.1.96;
GN   OrderedLocusNames=MT1196;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin =
CC         (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96;
CC   -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45453.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003406082.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WI92; -.
DR   SMR; P9WI92; -.
DR   EnsemblBacteria; AAK45453; AAK45453; MT1196.
DR   GeneID; 45425131; -.
DR   KEGG; mtc:MT1196; -.
DR   PATRIC; fig|83331.31.peg.1296; -.
DR   HOGENOM; CLU_081974_4_3_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1360.20; -; 1.
DR   HAMAP; MF_00434; Pterin_4_alpha; 1.
DR   InterPro; IPR036428; PCD_sf.
DR   InterPro; IPR001533; Pterin_deHydtase.
DR   PANTHER; PTHR12599; PTHR12599; 1.
DR   Pfam; PF01329; Pterin_4a; 1.
DR   SUPFAM; SSF55248; SSF55248; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..94
FT                   /note="Putative pterin-4-alpha-carbinolamine dehydratase"
FT                   /id="PRO_0000428047"
SQ   SEQUENCE   94 AA;  10380 MW;  21F1A514995CE65A CRC64;
     MAVLTDEQVD AALHDLNGWQ RAGGVLRRSI KFPTFMAGID AVRRVAERAE EVNHHPDIDI
     RWRTVTFALV THAVGGITEN DIAMAHDIDA MFGA
 
 
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