Reviewed, UniProtKB/Swiss-Prot B0C7G7 (F16A2_ACAM1)

Names and origin

Protein names

Recommended name:
    Fructose-1,6-bisphosphatase class 1 2
      Short name=FBPase class 1 2
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 2

Gene names

Name:	fbp2
Ordered Locus Names:	AM1_6321

Organism

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

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Acaryochloris

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. HAMAP MF_01855
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Pathway	Carbohydrate biosynthesis; Calvin cycle. HAMAP MF_01855
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the FBPase class 1 family.

Ontologies

Keywords
Biological process	Calvin cycle Carbohydrate metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 331	331	Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855		PRO_0000364442
Regions
	Region	115 – 118	4	Substrate binding By similarity
Sites
	Metal binding	91	1	Magnesium 1 By similarity
	Metal binding	112	1	Magnesium 1 By similarity
	Metal binding	112	1	Magnesium 2 By similarity
	Metal binding	114	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	115	1	Magnesium 2 By similarity
	Metal binding	274	1	Magnesium 2 By similarity
	Binding site	207	1	Substrate By similarity
	Binding site	238	1	Substrate By similarity
	Binding site	268	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0C7G7-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 153AB30769EBAC77	FASTA	331	36,121
	10 20 30 40 50 60 MSHPTTFNSH LWQQHRLAQQ PIEISILLTQ MGFAAKVLAR EISRAALMGN LGLMGETNAT 70 80 90 100 110 120 GDAQKKLDVF SNQIVIDAFS NIGLVAVIAS EELDQVKLIE CGQQAQYILC TDPLDGSSNT 130 140 150 160 170 180 DTGSAVGTIF GIYRRQTSGY CSTEADVLQP GTELVTAGYV LYGTSTMLVY TTGGRVDGFT 190 200 210 220 230 240 LDPSLGEFLL SHENIRCPET GKTYSANLSY YQEWHPHIQN FADYLSDRKS HTAHTLRYSG 250 260 270 280 290 300 ALVADVHRCL LEGGLYFYPP TADQPEGKLR LLYECAPLAF LVEQAGGKAT SGLARIMDLE 310 320 330 VTSIHQRSPL VIGSQVAVNL YQTFLEQGKA A

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000828 Genomic DNA. Translation: ABW31251.1.
RefSeq	YP_001520570.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5685098.
GenomeReviews	Gene locus AM1_6321 in contig CP000828_GR.
KEGG	amr:AM1_6321.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	IVTFDPL.
Family and domain databases
HAMAP	MF_01855. [Tree]
InterPro	IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. F16BPHPHTASE.
ProDom	PD001491. In_FB_phphtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F16A2_ACAM1

Accession

Primary (citable) accession number: B0C7G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	February 26, 2008
Last modified:	November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)