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Database: UniProt
Entry: Q5FSE8_GLUOX
LinkDB: Q5FSE8_GLUOX
Original site: Q5FSE8_GLUOX 
ID   Q5FSE8_GLUOX            Unreviewed;       626 AA.
AC   Q5FSE8;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 119.
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   OrderedLocusNames=GOX0926 {ECO:0000313|EMBL:AAW60698.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60698.1, ECO:0000313|Proteomes:UP000006375};
RN   [1] {ECO:0000313|EMBL:AAW60698.1, ECO:0000313|Proteomes:UP000006375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H {ECO:0000313|EMBL:AAW60698.1,
RC   ECO:0000313|Proteomes:UP000006375};
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60698.1; -; Genomic_DNA.
DR   RefSeq; WP_011252493.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FSE8; -.
DR   STRING; 290633.GOX0926; -.
DR   KEGG; gox:GOX0926; -.
DR   eggNOG; COG0529; Bacteria.
DR   eggNOG; COG2895; Bacteria.
DR   HOGENOM; CLU_007265_5_3_5; -.
DR   OMA; DWYGGPT; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000006375; 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: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:RHEA.
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   CDD; cd03695; CysN_NodQ_II; 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; IPR044138; CysN_II.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
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; 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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00065}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000313|EMBL:AAW60698.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00065}; Nucleotidyltransferase {ECO:0000313|EMBL:AAW60698.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000313|EMBL:AAW60698.1}.
FT   DOMAIN          16..227
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   626 AA;  67691 MW;  5CAE9F45E231E668 CRC64;
     MGDNIVTESF SETHRAAATP IVIVGHVDHG KSTLIGRLLY DTDSLQDGKL AQIVESSRKR
     GLAVEWSFLL DSLQIERDQG VTVDSTRIPF RLGSREFVIV DAPGHRQFLR NMITGAADAE
     AAVLVVDAKE GAQEQTRRHA MLLRLIGIRH VIVLLNKSDI LGFDEAQIVK VESDVRQLLG
     RLEIEVEAVV PASARDGDNI ASRSERSLWY KGPTLVEALA NVPPPASRAA LPFRMPVQDV
     YRFDGIRYVA GRIERGTVRA GDRLSIGAQG QVATVAEVCR WHAPELPVAG AGESIALRLE
     PDLVPDRGDL LFPADDQAAA PERSARIRTR LFWLRGEPLR VGESFTLRLA TAEHDVTVAS
     IDAVVDLEDL TLREGDSVPP DGFAEITLAA SHAVLFDPFS PGFGDGRGVL VDRYQRIVGG
     APLIGPAELA DGEHAIHPTA SRVSAARQVQ TRGHKSGVFW LTGLPGSGKS TVARAAELAL
     SEQAINATVL DGDTLRAGLC SDLGFSPEDR HENIRRAAHV AKILAESGQV VIVALVSPLQ
     ADRAQARQIV GENFHEVFVD TPLETCEKRD PKGLYAAARA GKIPEFTGIS APYEAPVSPE
     LRLPADRPEQ EAINTLTAFI LRIVQP
//
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