SATC1_SORC5
ID SATC1_SORC5 Reviewed; 578 AA.
AC A9ENT2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Probable bifunctional SAT/APS kinase 1;
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;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE Includes:
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=sat1/cysC1; OrderedLocusNames=sce0740;
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56;
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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 -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; AM746676; CAN90897.1; -; Genomic_DNA.
DR AlphaFoldDB; A9ENT2; -.
DR SMR; A9ENT2; -.
DR STRING; 448385.sce0740; -.
DR EnsemblBacteria; CAN90897; CAN90897; sce0740.
DR KEGG; scl:sce0740; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_438653_0_0_7; -.
DR UniPathway; UPA00140; UER00204.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000002139; 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: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 CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR HAMAP; MF_00066; Sulf_adenylyltr; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020792; SO4_adenylyltransferase_pro.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..578
FT /note="Probable bifunctional SAT/APS kinase 1"
FT /id="PRO_0000340641"
FT REGION 1..192
FT /note="Adenylsulfate kinase"
FT REGION 193..578
FT /note="Sulfate adenylyltransferase"
FT ACT_SITE 87
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 63587 MW; A63606BD70A9A164 CRC64;
MASGEGFVVW FTGLSGSGKS TLAAMLAAEL PRRGVHVESL DGDVVRTHLS KGLGFSREDR
DTNIRRIGFV ARLVARSGAC AITAAISPYR EIRDEQRRAI GRFCEVYCEC PLDVLERRDI
KGLYARARAG EIKGFTGVDD PYEPPRSPEV IVHTDRESPR EGLARILAKL EELGYVRPMA
QPAEPARAGL APPHGGELVD RFVRGDARQR LLERVAGLPR VRLDERGASD LELIGNGAYS
PLKGFMTSRD YLRVVRERRL ESGLVWSIPI TLAVPGEDAA RLSLGSEVAL ASPDGRVVGV
LELVDRWTPD KEVEARNVYG ATDEGHPGVA YLRSSGDVYL GGEVWLIERP LSPQFPEYPR
DPAATRAAFE ARGWRRVVGF QTRNPIHRAH EHITKCALEI TDGLLLHPLV GATKAGDIPA
DVRMRCYELL LEKYYPADRV VLGLYPAAMR YAGPREAIFH ALVRKNYGCS HFIVGRDHAG
VGRFYGTYDA QRAFDDFLPS ELGIEPLKFE EAFWSTVVGG MATDKTAPGG PETRITLSGT
QVRELLRAGK LPPPEFSRPE VAQILLSATQ GRGHDQAA
