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Protein

Bifunctional enzyme CysN/CysC

Gene

cysNC

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity.By similarity
APS kinase catalyzes the synthesis of activated sulfate.By similarity

Catalytic activityi

ATP + sulfate = diphosphate + adenylyl sulfate.
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 1 and 2 of the subpathway that synthesizes sulfite from sulfate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Bifunctional enzyme CysN/CysC (cysNC), Sulfate adenylyltransferase subunit 2 (cysD), Sulfate adenylyltransferase subunit 2 (cysD)
  2. Bifunctional enzyme CysN/CysC (cysNC)
  3. Phosphoadenosine phosphosulfate reductase (cysH), Probable phosphoadenosine phosphosulfate reductase (cysH)
This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sulfite from sulfate, the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei524Phosphoserine intermediateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 18GTPBy similarity8
Nucleotide bindingi88 – 92GTPBy similarity5
Nucleotide bindingi143 – 146GTPBy similarity4
Nucleotide bindingi450 – 457ATPSequence analysis8

GO - Molecular functioni

  • adenylylsulfate kinase activity Source: MTBBASE
  • ATP binding Source: UniProtKB-KW
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • sulfate adenylyltransferase (ATP) activity Source: UniProtKB-EC

GO - Biological processi

  • cellular response to oxidative stress Source: MTBBASE
  • cellular response to sulfur starvation Source: MTBBASE
  • growth Source: MTBBASE
  • hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  • sulfate assimilation Source: Reactome
  • sulfate assimilation via adenylyl sulfate reduction Source: MTBBASE

Keywords - Molecular functioni

Kinase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-5458-MONOMER.
ReactomeiR-MTU-936635. Sulfate assimilation.
UniPathwayiUPA00140; UER00204.
UPA00140; UER00205.

Names & Taxonomyi

Protein namesi
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 namesi
Name:cysNC
Synonyms:cysN
Ordered Locus Names:Rv1286
ORF Names:MTCY373.05
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1286.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • plasma membrane Source: MTBBASE
  • sulfate adenylyltransferase complex (ATP) Source: MTBBASE

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000915371 – 614Bifunctional enzyme CysN/CysCAdd BLAST614

Proteomic databases

PaxDbiP9WNM5.

Expressioni

Inductioni

Induced by sulfur limitation and oxidative stress. Repressed by the presence of cysteine.1 Publication

Interactioni

Subunit structurei

Heterodimer composed of CysD, the smaller subunit, and CysNC.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv1286.

Structurei

Secondary structure

1614
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi444 – 449Combined sources6
Helixi456 – 469Combined sources14
Beta strandi474 – 476Combined sources3
Helixi479 – 482Combined sources4
Turni483 – 489Combined sources7
Helixi494 – 513Combined sources20
Beta strandi517 – 521Combined sources5
Helixi527 – 540Combined sources14
Beta strandi544 – 549Combined sources6
Helixi553 – 559Combined sources7
Helixi564 – 569Combined sources6
Turni577 – 579Combined sources3
Beta strandi590 – 593Combined sources4
Helixi599 – 611Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BZQX-ray2.10A/B440-612[»]
4BZXX-ray1.70A/B440-612[»]
4RFVX-ray1.69A/B424-612[»]
ProteinModelPortaliP9WNM5.
SMRiP9WNM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 217tr-type GAdd BLAST216

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 441Sulfate adenylyltransferaseAdd BLAST441
Regioni11 – 18G1By similarity8
Regioni67 – 71G2By similarity5
Regioni88 – 91G3By similarity4
Regioni143 – 146G4By similarity4
Regioni180 – 182G5By similarity3
Regioni442 – 614Adenylyl-sulfate kinaseAdd BLAST173

Sequence similaritiesi

In the C-terminal section; belongs to the APS kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105C3T. Bacteria.
COG0529. LUCA.
COG2895. LUCA.
KOiK00955.
OMAiMLVWMDE.
PhylomeDBiP9WNM5.

Family and domain databases

CDDicd02027. APSK. 1 hit.
Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00065. Adenylyl_sulf_kinase. 1 hit.
MF_00062. Sulf_adenylyltr_sub1. 1 hit.
InterProiIPR002891. APS_kinase.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR011779. SO4_adenylTrfase_lsu.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00455. apsK. 1 hit.
TIGR02034. CysN. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WNM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLLRLATA GSVDDGKSTL IGRLLYDSKA VMEDQWASVE QTSKDRGHDY
60 70 80 90 100
TDLALVTDGL RAEREQGITI DVAYRYFATP KRKFIIADTP GHIQYTRNMV
110 120 130 140 150
TGASTAQLVI VLVDARHGLL EQSRRHAFLA SLLGIRHLVL AVNKMDLLGW
160 170 180 190 200
DQEKFDAIRD EFHAFAARLD VQDVTSIPIS ALHGDNVVTK SDQTPWYEGP
210 220 230 240 250
SLLSHLEDVY IAGDRNMVDV RFPVQYVIRP HTLEHQDHRS YAGTVASGVM
260 270 280 290 300
RSGDEVVVLP IGKTTRITAI DGPNGPVAEA FPPMAVSVRL ADDIDISRGD
310 320 330 340 350
MIARTHNQPR ITQEFDATVC WMADNAVLEP GRDYVVKHTT RTVRARIAGL
360 370 380 390 400
DYRLDVNTLH RDKTATALKL NELGRVSLRT QVPLLLDEYT RNASTGSFIL
410 420 430 440 450
IDPDTNGTVA AGMVLRDVSA RTPSPNTVRH RSLVTAQDRP PRGKTVWFTG
460 470 480 490 500
LSGSGKSSVA MLVERKLLEK GISAYVLDGD NLRHGLNADL GFSMADRAEN
510 520 530 540 550
LRRLSHVATL LADCGHLVLV PAISPLAEHR ALARKVHADA GIDFFEVFCD
560 570 580 590 600
TPLQDCERRD PKGLYAKARA GEITHFTGID SPYQRPKNPD LRLTPDRSID
610
EQAQEVIDLL ESSS
Length:614
Mass (Da):67,839
Last modified:April 16, 2014 - v1
Checksum:i2C3709C8B91867C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44042.1.
PIRiB70772.
RefSeqiNP_215802.1. NC_000962.3.
WP_003406621.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44042; CCP44042; Rv1286.
GeneIDi886978.
KEGGimtu:Rv1286.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44042.1.
PIRiB70772.
RefSeqiNP_215802.1. NC_000962.3.
WP_003406621.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BZQX-ray2.10A/B440-612[»]
4BZXX-ray1.70A/B440-612[»]
4RFVX-ray1.69A/B424-612[»]
ProteinModelPortaliP9WNM5.
SMRiP9WNM5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1286.

Proteomic databases

PaxDbiP9WNM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44042; CCP44042; Rv1286.
GeneIDi886978.
KEGGimtu:Rv1286.

Organism-specific databases

TubercuListiRv1286.

Phylogenomic databases

eggNOGiENOG4105C3T. Bacteria.
COG0529. LUCA.
COG2895. LUCA.
KOiK00955.
OMAiMLVWMDE.
PhylomeDBiP9WNM5.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00204.
UPA00140; UER00205.
BioCyciMTBH37RV:G185E-5458-MONOMER.
ReactomeiR-MTU-936635. Sulfate assimilation.

Family and domain databases

CDDicd02027. APSK. 1 hit.
Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00065. Adenylyl_sulf_kinase. 1 hit.
MF_00062. Sulf_adenylyltr_sub1. 1 hit.
InterProiIPR002891. APS_kinase.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR011779. SO4_adenylTrfase_lsu.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00455. apsK. 1 hit.
TIGR02034. CysN. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYSNC_MYCTU
AccessioniPrimary (citable) accession number: P9WNM5
Secondary accession number(s): L0T6E9, Q10600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 23 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

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.