ID I2QMK9_9BRAD Unreviewed; 638 AA.
AC I2QMK9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=Bra1253DRAFT_05784 {ECO:0000313|EMBL:EIG61015.1};
OS Bradyrhizobium sp. WSM1253.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319003 {ECO:0000313|EMBL:EIG61015.1, ECO:0000313|Proteomes:UP000005125};
RN [1] {ECO:0000313|EMBL:EIG61015.1, ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|EMBL:EIG61015.1,
RC ECO:0000313|Proteomes:UP000005125};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "Improved High-Quality Draft sequence of Bradyrhizobium sp. WSM1253.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|Proteomes:UP000005125};
RX PubMed=26629308;
RA Tiwari R., Howieson J., Yates R., Tian R., Held B., Tapia R., Han C.,
RA Seshadri R., Reddy T.B., Huntemann M., Pati A., Woyke T., Markowitz V.,
RA Ivanova N., Kyrpides N., Reeve W.;
RT "Genome sequence of Bradyrhizobium sp. WSM1253; a microsymbiont of
RT Ornithopus compressus from the Greek Island of Sifnos.";
RL Stand. Genomic Sci. 10:113-113(2015).
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; JH600073; EIG61015.1; -; Genomic_DNA.
DR RefSeq; WP_007599836.1; NZ_JH600073.1.
DR AlphaFoldDB; I2QMK9; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_3_5; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000005125; 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; cd04095; CysN_NoDQ_III; 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; 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 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; PS00301; G_TR_1; 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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EIG61015.1};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT DOMAIN 18..230
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT ACT_SITE 537
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 463..470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 638 AA; 69153 MW; 67ACAE8D55C2C3E7 CRC64;
MNMIVTPASP ATPNGTTRPQ VRIVIVGHVD HGKSTLVGRL LHETGSLPDG KLDMLKAVSA
RRGMPFEWSF LLDALQTERD QGITIDTTQI RFRTNSRDIV LIDAPGHAEF LRNMITGASQ
ADGAVLIIDA LEGVRDQTRR HGYLLHLLGV KQVAVVVNKM DRVDFSAERF KEISDEISAH
LQGLGVKPTA VIPISARDGD GVAERTDRID WYKGPTVVEA LDRLEPARPL EALALRLPVQ
AIYKFDDRRI VAGRIESGSL VAGDEIVIMP AGKIARIKTV ESWPVTPVAG RQGAGRSVGI
TLDRELFLER GDIIAHTNSA PRETRRLRAR IFWLHDKPLA KGDQLLVRCG PKESRATVVA
IEKAVDPGEL SSVENKAIGR NHVGEIDISL SNPIATDPYT ENPRTGRLVI EVSGRIAGGG
LVLSVDAGQR ALPVDIVPVE SALRPDERSA RYRHNGAVVW LTGLPASGKS TLAKALERRL
FSNGGSPILL DGDTLRAGLN SDLGFSAADR SENIRRLAEV ATHLARNGHI AIVAAVSPAR
EDRATARRIA DTAFREIHVA TPAEICEERD PKGHYKKARA GTLASFTGIG NDYETPQAAE
LVIDTSTRTV AEAADEIERM LKTTGVLFDE LVDLAANI
//
