FAPD_ALKHC
ID FAPD_ALKHC Reviewed; 427 AA.
AC Q9K9G9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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}; OrderedLocusNames=BH2678;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine
CC {ECO:0000269|PubMed:17618314};
CC Note=kcat is 14 min(-1). {ECO:0000269|PubMed:17618314};
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; BA000004; BAB06397.1; -; Genomic_DNA.
DR PIR; F83984; F83984.
DR RefSeq; WP_010898827.1; NC_002570.2.
DR AlphaFoldDB; Q9K9G9; -.
DR SMR; Q9K9G9; -.
DR STRING; 272558.10175299; -.
DR EnsemblBacteria; BAB06397; BAB06397; BAB06397.
DR KEGG; bha:BH2678; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_0_2_9; -.
DR OMA; WAVTKSY; -.
DR OrthoDB; 906744at2; -.
DR BioCyc; MetaCyc:MON-16806; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001258; 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; Hydrolase; Metal-binding; Reference proteome;
KW Thiamine biosynthesis; Zinc.
FT CHAIN 1..427
FT /note="N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine
FT deformylase"
FT /id="PRO_0000387966"
FT ACT_SITE 93
FT /evidence="ECO:0000250"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 47340 MW; 9ED35EC1E2236C39 CRC64;
MFKLSVIEEL LAHVDKNKEE LLALVQTLVA YPTPSPPARN TADAQQYIRT YCEKLGCNVD
MWDVYPNDPN VVAVLKGTYS ESYRSLILNG HIDVAAVDES EEWKTPPFEA TVNQGVIRGR
GVADMKGGLA ACLFAMKTLH AFNIQLPGDL IFQSVVGEEV GEAGTKSCCE RGYTADLAIV
SDTSHCEIQG QGGVITGWIT VKSPVTFHDG TRRNLIHAGG GEFGASAIEK MMKLIQGLQE
LERHWAVTKS SPGFPPGMNT INPAFIEGGR HPAFIADECK LWITIHYYPH ESYEEIVREV
EEHLLHVAKA DPWMREHPPS FSWGGTSMIE DKGEIFPAFQ IDEQSDAVQL LKKIHYHLTG
EEVKTSMSQT VTDGGWLAEA GIPTLLFGPG KLEDAHSVNE ELEIAELVQY TKTLLTFIYE
WCHLRKA
