ID A0A146G5F9_TERSA Unreviewed; 653 AA.
AC A0A146G5F9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=TSACC_2455 {ECO:0000313|EMBL:GAT32058.1};
OS Terrimicrobium sacchariphilum.
OC Bacteria; Verrucomicrobiota; Terrimicrobiia; Terrimicrobiales;
OC Terrimicrobiaceae; Terrimicrobium.
OX NCBI_TaxID=690879 {ECO:0000313|EMBL:GAT32058.1, ECO:0000313|Proteomes:UP000076023};
RN [1] {ECO:0000313|Proteomes:UP000076023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Terrimicrobium sacchariphilum strain NM-5.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Terrimicrobium sacchariphilum NM-5(T), a
RT facultative anaerobic soil bacterium of the class Spartobacteria.";
RL Genome Announc. 0:0-0(2017).
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 -!- 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; Evidence={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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAT32058.1}.
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DR EMBL; BDCO01000002; GAT32058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A146G5F9; -.
DR STRING; 690879.TSACC_2455; -.
DR InParanoid; A0A146G5F9; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000076023; 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; IPR005225; Small_GTP-bd_dom.
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 NCBIfam; TIGR00231; small_GTP; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT DOMAIN 20..233
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT ACT_SITE 545
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 653 AA; 72376 MW; 4C391B2FEE619D1A CRC64;
MQTTLEPTKV PTSDISLPTS QKLRIVIVGH VDHGKSTLIG RLFHDTNSLP EGKVEQIRKA
SELEGMEFEF AFLLDALLEE QAQNITIDTT QLPFRTDKRE YVIIDAPGHK EFLKNMVTGA
ASADAAILLI DANEGIQEQS KRHAYLLSLL GIRQIVVAVN KMDLVGYRQE RFEKVRADYT
EFLGKLGIVP QHFVPMSAKL GLNITTASPE LAWHKGPAIL EALEQFQISA PPDDLPLRFV
LQDIYRFDER RILAGRIETG SLQVGQEIVF WPDGKSSRVK SIEEWNAPEP PTSALVGESV
AITLEEQIFV ERGDIGSAPD HGPAEGREIQ ASLFWLQNDP LPLNVPFTLK LGTQSVEARL
VEITRVLDSS TLEPLAGNPG IIHKNEVADV RIRARKPIAF DRHDRISETG RFVIVTGKRI
GGGGIIREAE YQDEKRLAGA TENLTWTVSP VTRELRAENF GHRGAVLWLT GLSGSGKSTL
ATGLEYHLHR RGIFSYILDG DNLRHGLCAN LGFSAEDRSE NIRRAGETAR LMAEAGLVVI
CSLISPFRAD RDNVRKICQR DGIPFAEVFI NAPLDVCESR DPRGLYKKAR SGEIKEFTGI
TSPYEAPLAP ELELRTAEHT LDNTLLDLTH FAVDLSRIPE PQIDEELARG GGI
//
