B9MR32 (B9MR32_ANATD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Guanylate kinase EMBL ACM60136.1
EC=2.7.4.8 EMBL ACM60136.1

Gene names

Ordered Locus Names:

Athe_1035

Organism

Anaerocellum thermophilum (strain DSM 6725 / Z-1320) [Complete proteome] [HAMAP]

Taxonomic identifier

521460 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Essential for recycling GMP and indirectly, cGMP By similarity. SAAS SAAS020590
Catalytic activity	ATP + GMP = ADP + GDP. SAAS SAAS020590
Subcellular location	Cytoplasm By similarity SAAS SAAS020590.
Sequence similarities	Contains 1 guanylate kinase-like domain. SAAS SAAS017665

Ontologies

Keywords
Cellular component	Cytoplasm SAAS SAAS020590
Ligand	ATP-binding SAAS SAAS020590 Nucleotide-binding
Molecular function	Kinase SAAS SAAS020590 EMBL ACM60136.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine nucleotide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW guanylate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B9MR32 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: B9641E5E2B07A078	FASTA	199	22,916
	10 20 30 40 50 60 MREGLLIVIS GPAGTGKGTV VGRLLEKNPN IKLSISKTTR KPRPGEKEGV NYFFVSREQF 70 80 90 100 110 120 EEEIKNERFL EYAEYNNNYY GTPKDFVFEA LGKGYDVILE IETKGALQIK KVFSDAVLIF 130 140 150 160 170 180 LLPPSIEELY KRLVKRGTES EDEIRARLEI AKNEIKLVPE YDYCVINDNV DDAAEKIQKI 190 IEVEKLKSRR FDIQSFLKE

References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001393 Genomic DNA. Translation: ACM60136.1.
RefSeq	YP_002572909.1. NC_012034.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B9MR32.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7409592.
GenomeReviews	Gene locus Athe_1035 in contig CP001393_GR.
KEGG	ate:Athe_1035.
PATRIC	20899176. VBIAnaThe135187_1101.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	DIDWQGT.
ProtClustDB	PRK00300.
Family and domain databases
HAMAP	MF_00328. Guanylate_kinase. [Tree]
InterPro	IPR008144. Guanylate_kin. IPR008145. Guanylate_kin/L-typ_Ca_channel. IPR020590. Guanylate_kinase_CS. IPR017665. Guanylate_kinase_sub. [Graphical view]
KO	K00942.
Pfam	PF00625. Guanylate_kin. 1 hit. [Graphical view]
SMART	SM00072. GuKc. 1 hit. [Graphical view]
TIGRFAMs	TIGR03263. Guanyl_kin. 1 hit.
PROSITE	PS00856. GUANYLATE_KINASE_1. 1 hit. PS50052. GUANYLATE_KINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B9MR32_ANATD

Accession

Primary (citable) accession number: B9MR32

Entry history

Integrated into UniProtKB/TrEMBL:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	December 14, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)