FAPD_BACSU
ID FAPD_BACSU Reviewed; 426 AA.
AC O31724;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine deformylase;
DE Short=Formylaminopyrimidine deformylase {ECO:0000303|PubMed:17618314};
DE EC=3.5.1.- {ECO:0000269|PubMed:17618314};
DE AltName: Full=Amidohydrolase YlmB {ECO:0000303|PubMed:17618314};
GN Name=ylmB {ECO:0000303|PubMed:17618314}; Synonyms=thiQ;
GN OrderedLocusNames=BSU15350;
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 SEQUENCE REVISION TO 72.
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=17618314; DOI=10.1038/nchembio.2007.13;
RA Jenkins A.H., Schyns G., Potot S., Sun G., Begley T.P.;
RT "A new thiamin salvage pathway.";
RL Nat. Chem. Biol. 3:492-497(2007).
CC -!- FUNCTION: Catalyzes the deformylation of the formylaminopyrimidine N-
CC formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the
CC corresponding aminopyrimidine. {ECO:0000269|PubMed:17618314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine = 4-
CC amino-5-aminomethyl-2-methylpyrimidine + formate;
CC Xref=Rhea:RHEA:46212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:63416, ChEBI:CHEBI:85895;
CC Evidence={ECO:0000269|PubMed:17618314};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000269|PubMed:17618314}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13409.2; -; Genomic_DNA.
DR RefSeq; NP_389418.2; NC_000964.3.
DR RefSeq; WP_003244730.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31724; -.
DR SMR; O31724; -.
DR STRING; 224308.BSU15350; -.
DR MEROPS; M20.A19; -.
DR PaxDb; O31724; -.
DR PRIDE; O31724; -.
DR EnsemblBacteria; CAB13409; CAB13409; BSU_15350.
DR GeneID; 940116; -.
DR KEGG; bsu:BSU15350; -.
DR PATRIC; fig|224308.179.peg.1673; -.
DR eggNOG; COG0624; Bacteria.
DR InParanoid; O31724; -.
DR OMA; WAVTKSY; -.
DR PhylomeDB; O31724; -.
DR BioCyc; BSUB:BSU15350-MON; -.
DR BioCyc; MetaCyc:BSU15350-MON; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01910; DapE-ArgE; 1.
PE 1: Evidence at protein level;
KW Cobalt; Coiled coil; Hydrolase; Metal-binding; Reference proteome;
KW Thiamine biosynthesis; Zinc.
FT CHAIN 1..426
FT /note="N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine
FT deformylase"
FT /id="PRO_0000387967"
FT COILED 1..31
FT /evidence="ECO:0000255"
FT ACT_SITE 91
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 47153 MW; 0AA7CBAD9577E931 CRC64;
MDQQIYSLQK KVEEHKEELI QLAKTLISYQ TPAPPARNTE GIQSWIAGYL NELGFSIDKW
DVYPGDPNVV GKLKGTDSAD YYSLIINGHV DVAEVKEDEE WKHDPFHPIE KNGLLIGRGA
SDMKGGMACV LFAVKLIREA SIELPGDLIL QSVIGEEVGE AGTLECCKRG YHADFAIVAD
TSDMHIQGQG GVITGWIEIK SSQTFHDGTR RNMIHAGGGT FGASAIEKMA KIIAGLGELE
RHWSIMKSYP GFKPGTNTIN PAVIEGGRHA AFIADECRLW ITVHFYPNET HDQVAAEIED
YVNRLSDSDI WLRENRPVFK WGGSSMIEDR GEIFPALEVD PGHPGVLALT ASHQKVKREC
PIIDVSQSVT DGGWLYDAGI PCVIYGPGDL HNAHSVNEKV SIEQLVEYTK IILDFIISWC
SRKKEQ
