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UniProtKB - O31724 (FAPD_BACSU)
Protein
N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine deformylase
Gene
ylmB
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Catalyzes the deformylation of the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine.
1 PublicationCatalytic activityi
Cofactori
: thiamine diphosphate biosynthesis Pathwayi
This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 89 | Zinc 1By similarity | 1 | |
Active sitei | 91 | By similarity | 1 | |
Metal bindingi | 122 | Zinc 1By similarity | 1 | |
Metal bindingi | 122 | Zinc 2By similarity | 1 | |
Active sitei | 156 | Proton acceptorBy similarity | 1 | |
Metal bindingi | 157 | Zinc 2By similarity | 1 | |
Metal bindingi | 180 | Zinc 1By similarity | 1 | |
Metal bindingi | 394 | Zinc 2By similarity | 1 |
GO - Molecular functioni
- hydrolase activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- thiamine biosynthetic process Source: UniProtKB-KW
- thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Hydrolase |
Biological process | Thiamine biosynthesis |
Ligand | Cobalt, Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | BSUB:BSU15350-MONOMER |
UniPathwayi | UPA00060 |
Protein family/group databases
MEROPSi | M20.A19 |
Names & Taxonomyi
Protein namesi | Recommended name: N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine deformylase (EC:3.5.1.-1 Publication)Short name: Formylaminopyrimidine deformylase1 Publication Alternative name(s): Amidohydrolase YlmB1 Publication |
Gene namesi | Name:ylmB1 Publication Synonyms:thiQ Ordered Locus Names:BSU15350 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000387967 | 1 – 426 | N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine deformylaseAdd BLAST | 426 |
Proteomic databases
PaxDbi | O31724 |
Family & Domainsi
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1 – 31 | Sequence analysisAdd BLAST | 31 |
Sequence similaritiesi
Belongs to the peptidase M20A family.Curated
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | COG0624, Bacteria |
InParanoidi | O31724 |
OMAi | WAVTKSY |
PhylomeDBi | O31724 |
Family and domain databases
InterProi | View protein in InterPro IPR010182, ArgE/DapE IPR036264, Bact_exopeptidase_dim_dom IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
SUPFAMi | SSF55031, SSF55031, 1 hit |
TIGRFAMsi | TIGR01910, DapE-ArgE, 1 hit |
i Sequence
Sequence statusi: Complete.
O31724-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDQQIYSLQK KVEEHKEELI QLAKTLISYQ TPAPPARNTE GIQSWIAGYL
60 70 80 90 100
NELGFSIDKW DVYPGDPNVV GKLKGTDSAD YYSLIINGHV DVAEVKEDEE
110 120 130 140 150
WKHDPFHPIE KNGLLIGRGA SDMKGGMACV LFAVKLIREA SIELPGDLIL
160 170 180 190 200
QSVIGEEVGE AGTLECCKRG YHADFAIVAD TSDMHIQGQG GVITGWIEIK
210 220 230 240 250
SSQTFHDGTR RNMIHAGGGT FGASAIEKMA KIIAGLGELE RHWSIMKSYP
260 270 280 290 300
GFKPGTNTIN PAVIEGGRHA AFIADECRLW ITVHFYPNET HDQVAAEIED
310 320 330 340 350
YVNRLSDSDI WLRENRPVFK WGGSSMIEDR GEIFPALEVD PGHPGVLALT
360 370 380 390 400
ASHQKVKREC PIIDVSQSVT DGGWLYDAGI PCVIYGPGDL HNAHSVNEKV
410 420
SIEQLVEYTK IILDFIISWC SRKKEQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB13409.2 |
RefSeqi | NP_389418.2, NC_000964.3 WP_003244730.1, NZ_JNCM01000035.1 |
Genome annotation databases
EnsemblBacteriai | CAB13409; CAB13409; BSU_15350 |
GeneIDi | 940116 |
KEGGi | bsu:BSU15350 |
PATRICi | fig|224308.179.peg.1673 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB13409.2 |
RefSeqi | NP_389418.2, NC_000964.3 WP_003244730.1, NZ_JNCM01000035.1 |
3D structure databases
AlphaFoldDBi | O31724 |
SMRi | O31724 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU15350 |
Protein family/group databases
MEROPSi | M20.A19 |
Proteomic databases
PaxDbi | O31724 |
Genome annotation databases
EnsemblBacteriai | CAB13409; CAB13409; BSU_15350 |
GeneIDi | 940116 |
KEGGi | bsu:BSU15350 |
PATRICi | fig|224308.179.peg.1673 |
Phylogenomic databases
eggNOGi | COG0624, Bacteria |
InParanoidi | O31724 |
OMAi | WAVTKSY |
PhylomeDBi | O31724 |
Enzyme and pathway databases
UniPathwayi | UPA00060 |
BioCyci | BSUB:BSU15350-MONOMER |
Family and domain databases
InterProi | View protein in InterPro IPR010182, ArgE/DapE IPR036264, Bact_exopeptidase_dim_dom IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
SUPFAMi | SSF55031, SSF55031, 1 hit |
TIGRFAMsi | TIGR01910, DapE-ArgE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | FAPD_BACSU | |
Accessioni | O31724Primary (citable) accession number: O31724 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 3, 2009 |
Last sequence update: | May 5, 2009 | |
Last modified: | May 25, 2022 | |
This is version 113 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families