B0BZH9 (PUR9_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
   EC=2.1.2.3
   Alternative name(s):
   AICAR transformylase
2. IMP cyclohydrolase
   EC=3.5.4.10
   Alternative name(s):
   ATIC
   IMP synthase
   Inosinicase

Gene names

Name:	purH
Ordered Locus Names:	AM1_5779

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP MF_00139 IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP MF_00139
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP MF_00139 Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.
Domain	The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP MF_00139
Sequence similarities	Belongs to the PurH family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: EC phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 524	524	Bifunctional purine biosynthesis protein PurH HAMAP MF_00139		PRO_1000076472

Sequences

	Sequence		Length	Mass (Da)
	B0BZH9 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: E979D0DFD30BA415	FASTA	524	55,848
	10 20 30 40 50 60 MTRLALLSTS DKTGLVELAQ QLVNEYGFTL VSSGGTAVTI EKAGLPVTKV SDYTGSPEIL 70 80 90 100 110 120 GGRVKTLHPR IHGGILARRS LESDVQDLTE NNIQGIDLVV VNLYPFEETI AKQKAQGITD 130 140 150 160 170 180 PDQALADAVE QIDIGGPTMI RAAAKNHAHV TVLCDPQQYA SYLQELKHGE GETSLPFRQA 190 200 210 220 230 240 CALKVFERMA SYDRAIATHL RQSLATTDSQ TQLSILGTAK QTLRYGENPH QNAVWYQESD 250 260 270 280 290 300 TASGWAAAQQ LQGKELSYNN LVDLEAARRV IAEFAQAETQ PTVAILKHNN PCGVAQGETL 310 320 330 340 350 360 LQAYEKALAA DSVSAFGGIV AMNRAIDTDT AQVLTKTFLE CIVAPECQPE AAAVLQAKSN 370 380 390 400 410 420 LRVLVLPDLV SGPAVTVKAI AGGWLAQAAD ETLTPPADWQ IVTQAKPTEA QLAELLFAWK 430 440 450 460 470 480 VVKHVKSNAI VVTKDHTTLG VGAGQMNRVG SVNIALQQAG EKAQGGTLAS DGFFPFDDSV 490 500 510 520 RTAAAAGITA IIQPGGSIRD KDSIQAADEL GIVMAFTGTR HFLH

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MBIC 11017.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000828 Genomic DNA. Translation: ABW30724.1.
RefSeq	YP_001520043.1. NC_009925.1.
3D structure databases
ProteinModelPortal	B0BZH9.
ModBase	Search...
Protein-protein interaction databases
STRING	B0BZH9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5684566.
GenomeReviews	Gene locus AM1_5779 in contig CP000828_GR.
KEGG	amr:AM1_5779.
PATRIC	20625520. VBIAcaMar40141_5365.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG498048.
OMA	FTGTRHF.
PhylomeDB	B0BZH9.
ProtClustDB	PRK00881.
Enzyme and pathway databases
BioCyc	AMAR329726:AM1_5779-MONOMER.
Family and domain databases
HAMAP	MF_00139. PurH. [Tree]
InterPro	IPR024051. AICAR_Tfase_dom. IPR002695. AICARFT_IMPCHas. IPR016193. Cytidine_deaminase-like. IPR011607. MGS-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.140.20. G3DSA:3.40.140.20. 2 hits. G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
KO	K00602.
PANTHER	PTHR11692. AICARFT_IMPCHas. 1 hit.
Pfam	PF01808. AICARFT_IMPCHas. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PIRSF	PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMART	SM00798. AICARFT_IMPCHas. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit. SSF52335. MGS-like_dom. 1 hit.
TIGRFAMs	TIGR00355. PurH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PUR9_ACAM1

Accession

Primary (citable) accession number: B0BZH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program