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Entry: A0A235GDN5_9NOCA
LinkDB: A0A235GDN5_9NOCA
Original site: A0A235GDN5_9NOCA 
ID   A0A235GDN5_9NOCA        Unreviewed;       614 AA.
AC   A0A235GDN5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=BDB13_4960 {ECO:0000313|EMBL:OYD71294.1};
OS   Rhodococcus sp. OK302.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD71294.1, ECO:0000313|Proteomes:UP000215121};
RN   [1] {ECO:0000313|EMBL:OYD71294.1, ECO:0000313|Proteomes:UP000215121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK302 {ECO:0000313|EMBL:OYD71294.1,
RC   ECO:0000313|Proteomes:UP000215121};
RA   Pelletier D.;
RT   "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL   Submitted (AUG-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   -!- 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:OYD71294.1}.
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DR   EMBL; NPJZ01000001; OYD71294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235GDN5; -.
DR   OrthoDB; 9804504at2; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000215121; 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   CDD; cd03695; CysN_NodQ_II; 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; IPR041757; CysN_GTP-bd.
DR   InterPro; IPR044138; CysN_II.
DR   InterPro; IPR044139; CysN_NoDQ_III.
DR   InterPro; IPR031157; G_TR_CS.
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; 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:OYD71294.1};
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:OYD71294.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   DOMAIN          2..215
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   ACT_SITE        525
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         451..458
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   614 AA;  68016 MW;  BC69B6E3F5C1A4C5 CRC64;
     MPQLLRVATA GSVDDGKSTL IGRLLYDSKS IFEDQLEAVE RTSRERGDEY ANLALLTDGL
     RAEREQGITI DVAHRYFATP HRKFIIADTP GHEQYTRNMV TGASTADLAL ILVDARKGVL
     EQTRRHAFLS TLLGIPHLVL CVNKMDLVGW SQERFEEIKE EFRQFAIKLD VHDLSFIPVS
     ALLGDNIVAR TENMDWYDGP SLLHHLEQVH IASDRNLIDA RFPVQYVIRP QNQTDADLHD
     FRGYAGTVAS GVFKPGDEVV VLPSGFTSTV KAVHGPGGTV IEEAFAPSAV CIELADNLDV
     SRGDQLCRLN NRPQVGQEID AMICWLTEQT TLSENNRYSL LHTTRSTKAQ IVRLDYRLDV
     NTLHRDESAE SLSLNEIGRI SIKTQQPLMF DPYRRNRVTG SFILVDETTG NTVAAGMING
     PTLKESRVVW HSSEVSRDER ATQGATVWLT GLSASGKSTI AVELERRLVA AGIPAYRLDG
     DNLRHGLNAD LGFGAADRAE NVRRVGSVAQ MFADSGAVAV ACLISPYRED RDRVRAAHEA
     AGLRFIEVYV DTPIEQCEAR DPKGMYAKAR AGEITGFTGV DDPYEVPERA ELIVRPENGT
     PTEIALRIME VLDR
//
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