ID   A0A2A2EQ13_9GAMM        Unreviewed;       644 AA.
AC   A0A2A2EQ13;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00062, ECO:0000256|HAMAP-Rule:MF_00065};
DE   Includes:
DE     RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00062};
DE              EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00062};
DE     AltName: Full=ATP-sulfurylase large subunit {ECO:0000256|HAMAP-Rule:MF_00062};
DE     AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00062};
DE              Short=SAT {ECO:0000256|HAMAP-Rule:MF_00062};
DE   Includes:
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   Synonyms=cysN {ECO:0000256|HAMAP-Rule:MF_00062};
GN   ORFNames=CK498_21750 {ECO:0000313|EMBL:PAU74748.1};
OS   Halomonas sp. WRN001.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=2032625 {ECO:0000313|EMBL:PAU74748.1, ECO:0000313|Proteomes:UP000217771};
RN   [1] {ECO:0000313|EMBL:PAU74748.1, ECO:0000313|Proteomes:UP000217771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRN001 {ECO:0000313|EMBL:PAU74748.1,
RC   ECO:0000313|Proteomes:UP000217771};
RA   Wang D., Zhang G.;
RT   "Halomonas alkalisoli sp. nov., isolated from saline alkaline soil.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00062}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00062, ECO:0000256|SAAS:SAAS01122058};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl
CC         sulfate + 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
CC       from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and
CC       CysN. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00065}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. CysN/NodQ
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PAU74748.1}.
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DR   EMBL; NSKB01000009; PAU74748.1; -; Genomic_DNA.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000217771; 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-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR   InterPro; IPR002891; APS_kinase.
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; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00455; apsK; 1.
DR   TIGRFAMs; TIGR02034; CysN; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 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_00062,
KW   ECO:0000256|SAAS:SAAS00444459};
KW   Complete proteome {ECO:0000313|Proteomes:UP000217771};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055993};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|SAAS:SAAS01092249, ECO:0000313|EMBL:PAU74748.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055970};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056011, ECO:0000313|EMBL:PAU74748.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056018, ECO:0000313|EMBL:PAU74748.1}.
FT   DOMAIN       22    245       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      31     38       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     110    114       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     165    168       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     484    491       ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
FT   ACT_SITE    558    558       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00065}.
SQ   SEQUENCE   644 AA;  71152 MW;  EF314788A5EF24BE CRC64;
     MSHSSPLIAD DIESYLKEHE NKDLLRFITC GSVDDGKSTL IGRLLHDSKM IYEDQLAAIT
     QASKTSGTTG DAVDLALLVD GLQSEREQGI TIDVAYRFFS TDKRKFIIAD TPGHEQYTRN
     MATGASTASL AIILIDARYG VQTQTRRHSF IADLLGIQHL VIAINKMDLV EFSEARYDEI
     VAQYQEVAAK LHAPDIRFIP LSALNGDNVV DPSQHTPWYR DASGAPGATL LQLLESVEIT
     HDQNLSDLRF PVQYVNRPNL DFRGYCGTLA AGILRPGQAV KALPSGKTSS VERIVTYDGD
     LDVAYPGQAI TLTLADEIDI SRGDWLVSAD AEVPLVVGFE ADIVWMHDTA LEPGKLYDLK
     LATRDLAGKV TAIDYQIDVN TLEHRHAEHL DLNSIARCSV ELTAPVPVDD YRKSPGTGSF
     IIIDRLTNVT VGAGMIHQPS DSETPYEYRA HDSKANVVWN RTSVTQAMRE QLNGHSGKCI
     WFTGLSGSGK STLANALEIE LNRRGYHTML LDGDNVRHGL CKDLGMGEED RGENIRRVGE
     VARLFAEAGI IVITAFISPF RKDRDAVRAL FDEDAFIEVH VDTPLDVCEQ RDPKGLYQKA
     REGKIKDFTG IDSPYEPPVH GEIVLKTMFD NEQALISKVI KHVL
//