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Multifunctional fusion protein [Includes: Sulfate adenylyltransferase subunit 1 (EC 2.7.7.4) (ATP-sulfurylase large subunit) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (APS kinase) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenosine-5'-phosphosulfate kinase)]

 A0A031K292_9SPHN        Unreviewed;       640 AA.
A0A031K292;
09-JUL-2014, integrated into UniProtKB/TrEMBL.
09-JUL-2014, sequence version 1.
13-FEB-2019, entry version 34.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00062, ECO:0000256|HAMAP-Rule:MF_00065};
Includes:
RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00062};
EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00062};
AltName: Full=ATP-sulfurylase large subunit {ECO:0000256|HAMAP-Rule:MF_00062};
AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00062};
Short=SAT {ECO:0000256|HAMAP-Rule:MF_00062};
Includes:
RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065};
AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
Synonyms=cysN {ECO:0000256|HAMAP-Rule:MF_00062};
ORFNames=BES08_04945 {ECO:0000313|EMBL:AOR76174.1},
BV97_01435 {ECO:0000313|EMBL:EZP83325.1};
Novosphingobium resinovorum.
Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
Sphingomonadaceae; Novosphingobium.
NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP83325.1, ECO:0000313|Proteomes:UP000024329};
[1] {ECO:0000313|EMBL:EZP83325.1, ECO:0000313|Proteomes:UP000024329}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KF1 {ECO:0000313|EMBL:EZP83325.1,
ECO:0000313|Proteomes:UP000024329};
Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
"Whole genome sequence of Novosphingobium resinovorum KF1.";
Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AOR76174.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SA1 {ECO:0000313|EMBL:AOR76174.1};
Seilhamer J.J.;
Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Proteomes:UP000094626}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SA1 {ECO:0000313|Proteomes:UP000094626};
PubMed=27851894; DOI=10.1016/j.jbiotec.2016.11.013;
Hegedus B., Kos P.B., Balint B., Maroti G., Gan H.M., Perei K.,
Rakhely G.;
"Complete genome sequence of Novosphingobium resinovorum SA1, a
versatile xenobiotic-degrading bacterium capable of utilizing
sulfanilic acid.";
J. Biotechnol. 241:76-80(2017).
-!- FUNCTION: Catalyzes the synthesis of activated sulfate.
{ECO:0000256|HAMAP-Rule:MF_00065}.
-!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity.
{ECO:0000256|HAMAP-Rule:MF_00062}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000256|HAMAP-
Rule:MF_00062, ECO:0000256|SAAS:SAAS01122058};
-!- CATALYTIC ACTIVITY:
Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl
sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
ChEBI:CHEBI:456216; EC=2.7.1.25; Evidence={ECO:0000256|HAMAP-
Rule:MF_00065};
-!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00062}.
-!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
from sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}.
-!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and
CysN. {ECO:0000256|HAMAP-Rule:MF_00062}.
-!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
Rule:MF_00065}.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. CysN/NodQ
subfamily. {ECO:0000256|HAMAP-Rule:MF_00062}.
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EMBL; CP017075; AOR76174.1; -; Genomic_DNA.
EMBL; JFYZ01000003; EZP83325.1; -; Genomic_DNA.
RefSeq; WP_008830320.1; NZ_JFYZ01000003.1.
EnsemblBacteria; AOR76174; AOR76174; BES08_04945.
EnsemblBacteria; EZP83325; EZP83325; BV97_01435.
KEGG; nre:BES08_04945; -.
PATRIC; fig|158500.4.peg.1473; -.
KO; K00955; -.
OrthoDB; 244339at2; -.
BioCyc; GCF_001742225:G1F70-994-MONOMER; -.
UniPathway; UPA00140; UER00204.
UniPathway; UPA00140; UER00205.
Proteomes; UP000024329; Unassembled WGS sequence.
Proteomes; UP000094626; Chromosome.
GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
CDD; cd02027; APSK; 1.
HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
InterPro; IPR002891; APS_kinase.
InterPro; IPR031157; G_TR_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011779; SO4_adenylTrfase_lsu.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR009000; Transl_B-barrel_sf.
InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
Pfam; PF00009; GTP_EFTU; 1.
PRINTS; PR00315; ELONGATNFCT.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF50465; SSF50465; 1.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR00455; apsK; 1.
TIGRFAMs; TIGR02034; CysN; 1.
PROSITE; PS00301; G_TR_1; 1.
PROSITE; PS51722; G_TR_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
ECO:0000256|SAAS:SAAS00444459};
Complete proteome {ECO:0000313|Proteomes:UP000024329,
ECO:0000313|Proteomes:UP000094626};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
ECO:0000256|SAAS:SAAS00055993};
Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
ECO:0000256|SAAS:SAAS01092249, ECO:0000313|EMBL:EZP83325.1};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062,
ECO:0000256|SAAS:SAAS00055993, ECO:0000256|SAAS:SAAS00444459};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062,
ECO:0000256|SAAS:SAAS00056011};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
Transferase {ECO:0000256|HAMAP-Rule:MF_00062, ECO:0000256|HAMAP-
Rule:MF_00065, ECO:0000256|SAAS:SAAS00056011,
ECO:0000256|SAAS:SAAS01092249, ECO:0000313|EMBL:EZP83325.1}.
DOMAIN 31 246 Tr-type G. {ECO:0000259|PROSITE:PS51722}.
NP_BIND 40 47 GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
NP_BIND 119 123 GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
NP_BIND 174 177 GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
NP_BIND 477 484 ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
ACT_SITE 551 551 Phosphoserine intermediate.
{ECO:0000256|HAMAP-Rule:MF_00065}.
SEQUENCE 640 AA; 70603 MW; 6D3E87A5E4194EA9 CRC64;
MADIDTKEAV YVTDKLIAED IDAYLVQHEH KTMLRFITCG SVDDGKSTLI GRLLYDSKMI
FEDQLDALTA DSKKVGTQGQ EIDFALLVDG LAAEREQGIT IDVAYRFFNT EKRKFIVADC
PGHEQYTRNM VTGASTADLA VILIDARKGV LVQTRRHSYL CHLIGIKNIV LAVNKMDLVD
YDQAVFDGIV KDYAEFARSI GIDSFTAMPI SGFKGDNITT PSANTPWYKG PTLVEHLETV
EVLSSVDADK PFRLPVQWVN RPNLDFRGFS GLIATGSVKP GDKIRVLPSG KTSAITRVVT
YDGDLDEAVA GQSVTVCFED EIDCSRGSVI SVADNPPQTA DQFESTIVWL ADEALIPGRA
YWLKLGTQQV SATVAEPKYT VNVNTMEHMA AKTLDLNAIG VAELTTDKQV VFEPYAENRT
LGGFILIDKM TNATVAAGML NFSLRRSQNV HWQAVDIDRK QHAGLKNQKP AVLWFTGLSG
SGKSTIANMV EKKLHRMNRH TFLLDGDNVR HGLNKDLGFT EADRIENIRR VGEVSKLMTD
AGLIVITAFI SPFQADREMV RAMLPEGEFI EVFIDTPLKV AEARDVKGLY KKARSGELKN
FTGIDSPYEA PRNPEVRIDT TVISPEEAAE LIVNTLLGDA


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