ID   A3UH10_9RHOB            Unreviewed;       632 AA.
AC   A3UH10;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=OA2633_07704 {ECO:0000313|EMBL:EAP90081.1};
OS   Oceanicaulis sp. HTCC2633.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Oceanicaulis.
OX   NCBI_TaxID=314254 {ECO:0000313|EMBL:EAP90081.1, ECO:0000313|Proteomes:UP000006011};
RN   [1] {ECO:0000313|EMBL:EAP90081.1, ECO:0000313|Proteomes:UP000006011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2633 {ECO:0000313|EMBL:EAP90081.1,
RC   ECO:0000313|Proteomes:UP000006011};
RX   PubMed=21036991; DOI=10.1128/JB.01267-10;
RA   Oh H.M., Kang I., Vergin K.L., Lee K., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of Oceanicaulis sp. strain HTCC2633, isolated from
RT   the Western Sargasso Sea.";
RL   J. Bacteriol. 193:317-318(2011).
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:SAAS01159104};
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:EAP90081.1}.
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DR   EMBL; AAMQ01000003; EAP90081.1; -; Genomic_DNA.
DR   RefSeq; WP_009801936.1; NZ_CH672428.1.
DR   STRING; 314254.OA2633_07704; -.
DR   EnsemblBacteria; EAP90081; EAP90081; OA2633_07704.
DR   eggNOG; ENOG4105C3T; Bacteria.
DR   eggNOG; COG0529; LUCA.
DR   eggNOG; COG2895; LUCA.
DR   OrthoDB; 244339at2; -.
DR   BioCyc; OSP314254:G11SI-1561-MONOMER; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000006011; 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   CDD; cd04166; CysN_ATPS; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR041757; CysN_GTP-bd.
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:SAAS01159110};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006011};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159120};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|SAAS:SAAS01092249, ECO:0000313|EMBL:EAP90081.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159098};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159099, ECO:0000313|EMBL:EAP90081.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006011};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159119, ECO:0000313|EMBL:EAP90081.1}.
FT   DOMAIN       20    233       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      29     36       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     108    112       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     163    166       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     466    473       ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
FT   ACT_SITE    540    540       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00065}.
SQ   SEQUENCE   632 AA;  69857 MW;  6D356DBA07285380 CRC64;
     MADDAIRAEV AERLTRAGEN GVLRVITCGS VDDGKSTLIG RLLYDSKLLF EDQIKVLERD
     SRKHGTAGEE IDFALLLDGL EAEREQGITI DVAYRFFNTE KRKFIVADTP GHEQYTRNMA
     TGASTADLAI ILVDARKGVL TQTKRHTYIA NMMGIRHAVL AVNKMDLVEH SRARFHEIVS
     EYLTIAEDLG FATITPIPIS ARYGDNIFSR SDAMKWHDGP TLMEHLERVD TNTEKEAAYA
     FRFPVQWVNR PNLDFRGFSG TVASGAVAPG DDVVVAHSGK AAKISRVVTA DGDLETASAG
     DAVTLVLDRE IDIARGDMLA DPQQRPEVSD QFAAEILWMT EEEMLPGRSY LLKAGGQVSP
     VSVTTLKHKL NVNSFEKEPG KSLKLNEIGV CTLSTSRPIA FDPYKDQRET GSFILIDRFT
     NQTVGAGMIE FSLRRASNIH THAMDVDKAR RADMKGQKPA VLWFTGLSGA GKSTIANLVE
     RKLAEAGRHT YSLDGDNVRH GLNKDLGFTD VDRVENIRRI GEVAKLFVDA GLIVTCSFIS
     PFRSERQMVR ELVDEAEFIE IFVDAPLEVC MQRDPKGLYK KAQAGEIKNF TGFDSPYEAP
     ESAEIHLKTG DLSAEDAAER VIETLIERGF IG
//