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B9MS89

- PUR9_CALBD

UniProt

B9MS89 - PUR9_CALBD

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Protein

Bifunctional purine biosynthesis protein PurH

Gene
purH, Athe_1445
Organism
Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciCBES521460:GH8H-1464-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:purH
Ordered Locus Names:Athe_1445
OrganismiCaldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum)
Taxonomic identifieri521460 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor
ProteomesiUP000007723: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Bifunctional purine biosynthesis protein PurHUniRule annotationPRO_1000122943Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi521460.Athe_1445.

Structurei

3D structure databases

ProteinModelPortaliB9MS89.

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

B9MS89-1 [UniParc]FASTAAdd to Basket

« Hide

MNKRAIISVY DKNGIVEFAK KLKEFGYDII STGGTMKYLT ENGIEVINIS    50
DVTRFPEILD GRVKTLHPNI HAGILAMKDN REHLETLKAL DILPIDMVVV 100
NLYPFKETIF KEDVTLDNVI ENIDIGGPTM IRAAAKNFKY TTVIVDPEDY 150
DIVAMEIEKN GEVSYETRFY LATKVFEYTS YYDSMIFNYF KHVRKDQSFS 200
KHFTVPLELL QYLRYGENPH QKACFYKISL PFIETSNIVN CTQLHGKELS 250
YNNILDSDSA IELLKEFDEP TCVAIKHNNP CAVASAENIN EAYKKVYESD 300
PISIFGGIVA FNRKVDKNVA EQLKKIFLEI VIAPEFDEDA LSILCSKKDL 350
RVLKLASLEK TDTFYDIKSV NGGALVQEKD RMLLADQLQV VTERKPSEKE 400
LEDLIFAWKV VKHVKSNAIV VAKDKMTLGI GTGQTNRIWA VEHAISRSRF 450
DLKGAVLASD AFFPFSDSVE AAGKAGISAI IQPGGSIRDK DSIEMANRFN 500
IAMVFTGMRH FRH 513
Length:513
Mass (Da):58,040
Last modified:March 24, 2009 - v1
Checksum:iDDB36EA33E928206
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001393 Genomic DNA. Translation: ACM60543.1.
RefSeqiYP_002573316.1. NC_012034.1.

Genome annotation databases

EnsemblBacteriaiACM60543; ACM60543; Athe_1445.
GeneIDi7408103.
KEGGiate:Athe_1445.
PATRICi20900000. VBIAnaThe135187_1513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001393 Genomic DNA. Translation: ACM60543.1 .
RefSeqi YP_002573316.1. NC_012034.1.

3D structure databases

ProteinModelPortali B9MS89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 521460.Athe_1445.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM60543 ; ACM60543 ; Athe_1445 .
GeneIDi 7408103.
KEGGi ate:Athe_1445.
PATRICi 20900000. VBIAnaThe135187_1513.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci CBES521460:GH8H-1464-MONOMER.

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1888 / DSM 6725 / Z-1320.

Entry informationi

Entry nameiPUR9_CALBD
AccessioniPrimary (citable) accession number: B9MS89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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