SATC_AQUAE
ID SATC_AQUAE Reviewed; 546 AA.
AC O67174;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable bifunctional SAT/APS kinase;
DE Includes:
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
DE Includes:
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25;
DE AltName: Full=APS kinase;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase;
GN Name=sat/cysC; OrderedLocusNames=aq_1081;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 -!- 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 -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07134.1; -; Genomic_DNA.
DR PIR; C70393; C70393.
DR RefSeq; NP_213737.1; NC_000918.1.
DR PDB; 2GKS; X-ray; 2.31 A; A/B=1-546.
DR PDBsum; 2GKS; -.
DR AlphaFoldDB; O67174; -.
DR SMR; O67174; -.
DR STRING; 224324.aq_1081; -.
DR EnsemblBacteria; AAC07134; AAC07134; aq_1081.
DR KEGG; aae:aq_1081; -.
DR PATRIC; fig|224324.8.peg.841; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_0_1_0; -.
DR InParanoid; O67174; -.
DR OMA; WHTPPAV; -.
DR OrthoDB; 1574819at2; -.
DR BRENDA; 2.7.1.25; 396.
DR BRENDA; 2.7.7.4; 396.
DR UniPathway; UPA00140; UER00204.
DR UniPathway; UPA00140; UER00205.
DR EvolutionaryTrace; O67174; -.
DR Proteomes; UP000000798; 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:0004781; F:sulfate adenylyltransferase (ATP) activity; IBA:GO_Central.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IBA:GO_Central.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IBA:GO_Central.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR HAMAP; MF_00066; Sulf_adenylyltr; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020792; SO4_adenylyltransferase_pro.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..546
FT /note="Probable bifunctional SAT/APS kinase"
FT /id="PRO_0000105948"
FT REGION 1..370
FT /note="Sulfate adenylyltransferase"
FT REGION 371..546
FT /note="Adenylsulfate kinase"
FT ACT_SITE 453
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 379..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 25..30
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 210..224
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 423..442
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 456..463
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 471..477
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:2GKS"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:2GKS"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:2GKS"
FT HELIX 527..540
FT /evidence="ECO:0007829|PDB:2GKS"
SQ SEQUENCE 546 AA; 62787 MW; 9D78E32791283581 CRC64;
MEKIKYLKSI QISQRSVLDL KLLAVGAFTP LDRFMGEEDY RNVVESMRLK SGTLFPIPIT
LPMEKEIAKD LKEGEWIVLR DPKNVPLAIM RVEEVYKWNL EYEAKNVLGT TDPRHPLVAE
MHTWGEYYIS GELKVIQLPK YYDFPEYRKT PKQVREEIKS LGLDKIVAFQ TRNPMHRVHE
ELTKRAMEKV GGGLLLHPVV GLTKPGDVDV YTRMRIYKVL YEKYYDKKKT ILAFLPLAMR
MAGPREALWH GIIRRNYGAT HFIVGRDHAS PGKDSKGKPF YDPYEAQELF KKYEDEIGIK
MVPFEELVYV PELDQYVEIN EAKKRNLKYI NISGTEIREN FLKQGRKLPE WFTRPEVAEI
LAETYVPKHK QGFCVWLTGL PCAGKSTIAE ILATMLQARG RKVTLLDGDV VRTHLSRGLG
FSKEDRITNI LRVGFVASEI VKHNGVVICA LVSPYRSARN QVRNMMEEGK FIEVFVDAPV
EVCEERDVKG LYKKAKEGLI KGFTGVDDPY EPPVAPEVRV DTTKLTPEES ALKILEFLKK
EGFIKD
