CYSNC_MYCTU
ID CYSNC_MYCTU Reviewed; 614 AA.
AC P9WNM5; L0T6E9; Q10600;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Bifunctional enzyme CysN/CysC;
DE Includes:
DE RecName: Full=Sulfate adenylyltransferase subunit 1;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase large subunit;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
DE Includes:
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25;
DE AltName: Full=APS kinase;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
GN Name=cysNC; Synonyms=cysN; OrderedLocusNames=Rv1286; ORFNames=MTCY373.05;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP SUBUNIT, AND INDUCTION.
RC STRAIN=Mt103;
RX PubMed=15184554; DOI=10.1099/mic.0.26894-0;
RA Pinto R., Tang Q.X., Britton W.J., Leyh T.S., Triccas J.A.;
RT "The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced
RT operon that encodes a tri-functional sulfate-activating complex.";
RL Microbiology 150:1681-1686(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the
CC adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC APS synthesis involves the formation of a high-energy phosphoric-
CC sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC to ATP hydrolysis by CysD. {ECO:0000250}.
CC -!- FUNCTION: APS kinase catalyzes the synthesis of activated sulfate.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysNC.
CC {ECO:0000269|PubMed:15184554}.
CC -!- INDUCTION: Induced by sulfur limitation and oxidative stress. Repressed
CC by the presence of cysteine. {ECO:0000269|PubMed:15184554}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class
CC translation factor GTPase superfamily. Classic translation factor
CC GTPase family. CysN/NodQ subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44042.1; -; Genomic_DNA.
DR PIR; B70772; B70772.
DR RefSeq; NP_215802.1; NC_000962.3.
DR RefSeq; WP_003406621.1; NZ_NVQJ01000030.1.
DR PDB; 4BZQ; X-ray; 2.10 A; A/B=440-612.
DR PDB; 4BZX; X-ray; 1.70 A; A/B=440-612.
DR PDB; 4RFV; X-ray; 1.69 A; A/B=424-612.
DR PDBsum; 4BZQ; -.
DR PDBsum; 4BZX; -.
DR PDBsum; 4RFV; -.
DR AlphaFoldDB; P9WNM5; -.
DR SMR; P9WNM5; -.
DR STRING; 83332.Rv1286; -.
DR PaxDb; P9WNM5; -.
DR DNASU; 886978; -.
DR GeneID; 45425258; -.
DR GeneID; 886978; -.
DR KEGG; mtu:Rv1286; -.
DR TubercuList; Rv1286; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG2895; Bacteria.
DR OMA; FPVQYVL; -.
DR PhylomeDB; P9WNM5; -.
DR BRENDA; 2.7.1.25; 3445.
DR Reactome; R-MTU-936635; Sulfate assimilation.
DR UniPathway; UPA00140; UER00204.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0009336; C:sulfate adenylyltransferase complex (ATP); IDA:MTBBASE.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IMP:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:MTBBASE.
DR GO; GO:0010438; P:cellular response to sulfur starvation; IEP:MTBBASE.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IDA:MTBBASE.
DR CDD; cd02027; APSK; 1.
DR CDD; cd04166; CysN_ATPS; 1.
DR CDD; cd03695; CysN_NodQ_II; 1.
DR CDD; cd04095; CysN_NoDQ_III; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR041757; CysN_GTP-bd.
DR InterPro; IPR044138; CysN_II.
DR InterPro; IPR044139; CysN_NoDQ_III.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR02034; CysN; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; GTP-binding; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..614
FT /note="Bifunctional enzyme CysN/CysC"
FT /id="PRO_0000091537"
FT DOMAIN 2..217
FT /note="tr-type G"
FT REGION 1..441
FT /note="Sulfate adenylyltransferase"
FT REGION 11..18
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 67..71
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 88..91
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 143..146
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 180..182
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 442..614
FT /note="Adenylyl-sulfate kinase"
FT REGION 578..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 524
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 450..457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:4RFV"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:4RFV"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:4RFV"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:4RFV"
FT TURN 483..489
FT /evidence="ECO:0007829|PDB:4RFV"
FT HELIX 494..513
FT /evidence="ECO:0007829|PDB:4RFV"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:4RFV"
FT HELIX 527..540
FT /evidence="ECO:0007829|PDB:4RFV"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:4RFV"
FT HELIX 553..559
FT /evidence="ECO:0007829|PDB:4BZX"
FT HELIX 564..569
FT /evidence="ECO:0007829|PDB:4BZX"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:4BZX"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:4RFV"
FT HELIX 599..611
FT /evidence="ECO:0007829|PDB:4RFV"
SQ SEQUENCE 614 AA; 67839 MW; 2C3709C8B91867C4 CRC64;
MTTLLRLATA GSVDDGKSTL IGRLLYDSKA VMEDQWASVE QTSKDRGHDY TDLALVTDGL
RAEREQGITI DVAYRYFATP KRKFIIADTP GHIQYTRNMV TGASTAQLVI VLVDARHGLL
EQSRRHAFLA SLLGIRHLVL AVNKMDLLGW DQEKFDAIRD EFHAFAARLD VQDVTSIPIS
ALHGDNVVTK SDQTPWYEGP SLLSHLEDVY IAGDRNMVDV RFPVQYVIRP HTLEHQDHRS
YAGTVASGVM RSGDEVVVLP IGKTTRITAI DGPNGPVAEA FPPMAVSVRL ADDIDISRGD
MIARTHNQPR ITQEFDATVC WMADNAVLEP GRDYVVKHTT RTVRARIAGL DYRLDVNTLH
RDKTATALKL NELGRVSLRT QVPLLLDEYT RNASTGSFIL IDPDTNGTVA AGMVLRDVSA
RTPSPNTVRH RSLVTAQDRP PRGKTVWFTG LSGSGKSSVA MLVERKLLEK GISAYVLDGD
NLRHGLNADL GFSMADRAEN LRRLSHVATL LADCGHLVLV PAISPLAEHR ALARKVHADA
GIDFFEVFCD TPLQDCERRD PKGLYAKARA GEITHFTGID SPYQRPKNPD LRLTPDRSID
EQAQEVIDLL ESSS
