ID A0A239ETN5_9PROT Unreviewed; 641 AA.
AC A0A239ETN5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
GN Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN ORFNames=SAMN05880556_105163 {ECO:0000313|EMBL:SNS48110.1};
OS Azospirillum sp. RU38E.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1907313 {ECO:0000313|EMBL:SNS48110.1, ECO:0000313|Proteomes:UP000198368};
RN [1] {ECO:0000313|EMBL:SNS48110.1, ECO:0000313|Proteomes:UP000198368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU38E {ECO:0000313|EMBL:SNS48110.1,
RC ECO:0000313|Proteomes:UP000198368};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: APS kinase catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|ARBA:ARBA00002357}.
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|HAMAP-Rule:MF_00065}.
CC -!- FUNCTION: Proposed to provide activated sulfate for transfer to Nod
CC factor. ATP sulfurylase may be the GTPase, regulating ATP sulfurylase
CC activity. {ECO:0000256|ARBA:ARBA00024872}.
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 Evidence={ECO:0000256|ARBA:ARBA00000262};
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 Evidence={ECO:0000256|ARBA:ARBA00001823, ECO:0000256|HAMAP-
CC Rule:MF_00065};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}.
CC -!- SUBUNIT: Sulfate-activating enzymes, NodP and NodQ, may be physically
CC associated. {ECO:0000256|ARBA:ARBA00011760}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00065}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC family. {ECO:0000256|ARBA:ARBA00005438}.
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:0000256|ARBA:ARBA00007237}.
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DR EMBL; FZOI01000005; SNS48110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239ETN5; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000198368; Unassembled WGS sequence.
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-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
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; cd04166; CysN_ATPS; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR041757; CysN_GTP-bd.
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 NCBIfam; TIGR00455; apsK; 1.
DR NCBIfam; TIGR02034; CysN; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00065}; Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW Reference proteome {ECO:0000313|Proteomes:UP000198368};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT DOMAIN 23..234
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT ACT_SITE 541
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 641 AA; 68619 MW; 24FA8120D1E97308 CRC64;
MAPAATLAAP RAEAPVLAPR KAQAPYPIVI VGHVDHGKST LIGRLLHDTD SLPEGRLAEL
QKVSSQRGLE LEWSFLLDAL QIERDQGITL DTTRIWFKTA KRPYVIIDAP GHREFLRNMV
TGASGADAAV LVTDAERGVS EQTRRHAYLL SLLGVTKVIV AVNKMDLMGH AEAAWQAVKD
EVSAYLAKLG MQPLYVIPLS ARHGDNIATR SQQMGWYQGP TLLEALDLLT PPAGRADATF
RMPIQDVYRR GDRRMAVGRI ETGRIRLGDK VEIAPTGQPA TVASIDTGRG DGEQFARAGQ
SAAISFIEDA ALARGQIIAP AGHMPHLALA LRVRAFWLDS EPLVVGSRLT LRLTTAEHAV
VVEKFERIVD VENLNDADTQ ELGQGGIAEI VLRSAAPIAF DPHTDLPITG RAGLARGTRI
VGGAVVLGAA ENAASVKGPV TAVDSSVDRA AFEARNGHRG GVLWLSGLSG AGKSTVAMGA
QRRLFDDGWR VLVLDGDNLR KGLNKDLGFS PAERLENVRR VAEVAKLMAE NGSVVLVSLI
SPTAELRALA RSIIGDGFHE VWVKADVNTC AQRDPKGLYA AARDGKIAQF TGVSAPFEAP
TSPDLVLDTA EFDIPTTTEL LIAHIRRNLA LDQADGHAVG I
//
