Bifunctional enzyme CysN/CysC - Mycobacterium tuberculosis

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Q10600 (CYSNC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional enzyme CysN/CysC

Including the following 2 domains:

Sulfate adenylyltransferase subunit 1
EC=2.7.7.4
Alternative name(s):
ATP-sulfurylase large subunit
Sulfate adenylate transferase
Short name=SAT
Adenylyl-sulfate kinase
EC=2.7.1.25
Alternative name(s):
APS kinase
ATP adenosine-5'-phosphosulfate 3'-phosphotransferase

Gene names

Name:	cysNC
Synonyms:	cysN
Ordered Locus Names:	Rv1286, MT1324
ORF Names:	MTCY373.05

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity By similarity. HAMAP MF_00062 APS kinase catalyzes the synthesis of activated sulfate By similarity. HAMAP MF_00062
Catalytic activity	ATP + sulfate = diphosphate + adenylyl sulfate. HAMAP MF_00062 ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate. HAMAP MF_00062
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. HAMAP MF_00062 Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Subunit structure	Heterodimer composed of CysD, the smaller subunit, and CysNC. Ref.3
Induction	Induced by sulfur limitation and oxidative stress. Repressed by the presence of cysteine. Ref.3
Sequence similarities	In the N-terminal section; belongs to the GTP-binding elongation factor family. CysN/nodQ subfamily. In the C-terminal section; belongs to the APS kinase family.

Ontologies

Keywords
Ligand	ATP-binding GTP-binding Nucleotide-binding
Molecular function	Kinase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Inferred from expression pattern Ref.3. Source: MTBBASE cellular response to sulfur starvation Inferred from expression pattern Ref.3. Source: MTBBASE growth Inferred from mutant phenotype. Source: MTBBASE sulfate assimilation via adenylyl sulfate reduction Inferred from direct assay Ref.3. Source: MTBBASE
Cellular component	cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay. Source: MTBBASE sulfate adenylyltransferase complex (ATP) Inferred from direct assay Ref.3. Source: MTBBASE
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro adenylylsulfate kinase activity Inferred from mutant phenotype. Source: MTBBASE sulfate adenylyltransferase (ATP) 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 – 614

614

Bifunctional enzyme CysN/CysC HAMAP MF_00062

PRO_0000091537

Regions

Nucleotide binding

11 – 18

GTP By similarity

Nucleotide binding

88 – 92

GTP By similarity

Nucleotide binding

143 – 146

GTP By similarity

Nucleotide binding

450 – 457

ATP Potential

Region

1 – 441

441

Sulfate adenylyltransferase HAMAP MF_00062

Region

442 – 614

173

Adenylyl-sulfate kinase HAMAP MF_00062

Sites

Active site

524

Phosphoserine intermediate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q10600 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2C3709C8B91867C4
Show »

FASTA

614

67,839

        10         20         30         40         50         60 
MTTLLRLATA GSVDDGKSTL IGRLLYDSKA VMEDQWASVE QTSKDRGHDY TDLALVTDGL 

        70         80         90        100        110        120 
RAEREQGITI DVAYRYFATP KRKFIIADTP GHIQYTRNMV TGASTAQLVI VLVDARHGLL 

       130        140        150        160        170        180 
EQSRRHAFLA SLLGIRHLVL AVNKMDLLGW DQEKFDAIRD EFHAFAARLD VQDVTSIPIS 

       190        200        210        220        230        240 
ALHGDNVVTK SDQTPWYEGP SLLSHLEDVY IAGDRNMVDV RFPVQYVIRP HTLEHQDHRS 

       250        260        270        280        290        300 
YAGTVASGVM RSGDEVVVLP IGKTTRITAI DGPNGPVAEA FPPMAVSVRL ADDIDISRGD 

       310        320        330        340        350        360 
MIARTHNQPR ITQEFDATVC WMADNAVLEP GRDYVVKHTT RTVRARIAGL DYRLDVNTLH 

       370        380        390        400        410        420 
RDKTATALKL NELGRVSLRT QVPLLLDEYT RNASTGSFIL IDPDTNGTVA AGMVLRDVSA 

       430        440        450        460        470        480 
RTPSPNTVRH RSLVTAQDRP PRGKTVWFTG LSGSGKSSVA MLVERKLLEK GISAYVLDGD 

       490        500        510        520        530        540 
NLRHGLNADL GFSMADRAEN LRRLSHVATL LADCGHLVLV PAISPLAEHR ALARKVHADA 

       550        560        570        580        590        600 
GIDFFEVFCD TPLQDCERRD PKGLYAKARA GEITHFTGID SPYQRPKNPD LRLTPDRSID 

       610 
EQAQEVIDLL ESSS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex." Pinto R., Tang Q.X., Britton W.J., Leyh T.S., Triccas J.A. Microbiology 150:1681-1686(2004) [PubMed: 15184554] [Abstract] Cited for: SUBUNIT, INDUCTION. Strain: Mt103.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842576 Genomic DNA. Translation: CAA97752.1. AE000516 Genomic DNA. Translation: AAK45585.1.
PIR	B70772.
RefSeq	NP_215802.1. NC_000962.2. NP_335771.1. NC_002755.2.
3D structure databases
ProteinModelPortal	Q10600.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000000459; EBMYCP00000000459; EBMYCG00000000459. EBMYCT00000071413; EBMYCP00000069472; EBMYCG00000071408.
GeneID	886978. 924747.
GenomeReviews	Gene locus MT1324 in contig AE000516_GR. Gene locus Rv1286 in contig AL123456_GR.
KEGG	mtc:MT1324. mtu:Rv1286.
PATRIC	18124676. VBIMycTub22151_1457.
TIGR	MT1324.
Organism-specific databases
TubercuList	Rv1286.
Phylogenomic databases
GeneTree	EBGT00050000014852.
HOGENOM	HBG307581.
OMA	GDMIARP.
PhylomeDB	Q10600.
ProtClustDB	PRK05506.
Enzyme and pathway databases
Reactome	REACT_27295. Mycobacterium tuberculosis biological processes.
Family and domain databases
HAMAP	MF_00062. Sulf_adenylyltr_sub1. Fused. [Tree] MF_00065. Adenylyl_sulf_kinase. Fused. [Tree]
InterPro	IPR002891. APS_kinase_C. IPR000795. ProtSyn_GTP-bd. IPR011779. SO4_adenylTrfase_lsu. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
KO	K00955.
Pfam	PF01583. APS_kinase. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SUPFAM	SSF50465. Elong_init_C. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00455. ApsK. 1 hit. TIGR02034. CysN. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSNC_MYCTU

Accession

Primary (citable) accession number: Q10600

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents