CYSNC_RHOBA
ID CYSNC_RHOBA Reviewed; 647 AA.
AC Q7UMW2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=cysC, cysN; OrderedLocusNames=RB7941;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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:0000250}.
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}.
CC -!- CAUTION: It is not obvious if the APS kinase domain is functional;
CC there is an Ala-555 replacing the conserved active site Ser.
CC Furthermore R.baltica seems to harbor a bona fide single domain APS
CC kinase (CysC). {ECO:0000305}.
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DR EMBL; BX294146; CAD75662.1; -; Genomic_DNA.
DR RefSeq; NP_868110.1; NC_005027.1.
DR RefSeq; WP_011121644.1; NC_005027.1.
DR AlphaFoldDB; Q7UMW2; -.
DR SMR; Q7UMW2; -.
DR STRING; 243090.RB7941; -.
DR EnsemblBacteria; CAD75662; CAD75662; RB7941.
DR KEGG; rba:RB7941; -.
DR PATRIC; fig|243090.15.peg.3838; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_3_0; -.
DR InParanoid; Q7UMW2; -.
DR OMA; DWYGGPT; -.
DR OrthoDB; 244339at2; -.
DR UniPathway; UPA00140; UER00204.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
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:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; GTP-binding; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..647
FT /note="Bifunctional enzyme CysN/CysC"
FT /id="PRO_0000239080"
FT DOMAIN 22..239
FT /note="tr-type G"
FT REGION 1..472
FT /note="Sulfate adenylyltransferase"
FT REGION 31..38
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 89..93
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 110..113
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 165..168
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 204..206
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 473..614
FT /note="Adenylyl-sulfate kinase"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 110..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 165..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 481..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 647 AA; 71170 MW; 59113B3A36831A31 CRC64;
MSHQSDLIAT DIDAYLKQHE QKQLLRFITC GSVDDGKSTL IGRLLYDSKL VYEDELAKVQ
SDSVRQGSVA GGFDPSLFMD GLKEEREQGI TIDVAYRYFS TAKRKFIIAD TPGHEQYTRN
MATGASSADL AIILIDARHG VLTQTRRHSF IVSLLGIRHV VVAVNKMDID GVDYSEDRFN
EICDDYRSFA TRLDLPDLHF IPISALNGDN LVDRSENMPW YTGSTLMNFL ETVYIGSDRN
LQDFRLPVQL VNRPNLNFRG FCGTIASGII RKGEEITVLP SRQKSKVKEI VTYDGNLDEA
YAPLAVTLTL EDEIDASRGD MIVRSGNLPR SESDVEAMLV WMNEEAMVPG KTYLVKHSTQ
TVPGNVETLA YKVDVNDLHR MPAPTLELNE IGRVRLSLSA PIHHDPYRRN RTTGAIILVD
RITNATVAAG MILDRGTTGS HKSVWDDEVS TDDSSDALST VTTEERAARF GQKPATVLLT
GLTGSGKTSI ARAVERKLFD AGRSVAVVDG EFVRRGLSRD LGFSADDRSE NLRRSGHLAH
TLNDAGLICL ASLVAPSDDV RQKVGKLIGE DQFLVVHVAT PLDVCRERDT KGQYAKADAG
ELSNFPGVTA KYDVPTNPDL AVDASTTSIA ECADAVVELL KLKGFIK
