ID G5B5S5_HETGA Unreviewed; 629 AA.
AC G5B5S5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 {ECO:0000313|EMBL:EHB04636.1};
GN ORFNames=GW7_16760 {ECO:0000313|EMBL:EHB04636.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB04636.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB04636.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC {ECO:0000256|ARBA:ARBA00005050}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00009290}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family. {ECO:0000256|ARBA:ARBA00007268}.
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DR EMBL; JH168597; EHB04636.1; -; Genomic_DNA.
DR AlphaFoldDB; G5B5S5; -.
DR STRING; 10181.G5B5S5; -.
DR eggNOG; KOG4238; Eukaryota.
DR InParanoid; G5B5S5; -.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0034033; P:purine nucleoside bisphosphate biosynthetic process; IEA:UniProt.
DR GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IEA:UniProt.
DR GO; GO:0034030; P:ribonucleoside bisphosphate biosynthetic process; IEA:UniProt.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniPathway.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 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; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR NCBIfam; TIGR00455; apsK; 1.
DR NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR PANTHER; PTHR11055:SF16; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE 2; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 237..390
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 398..620
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 71401 MW; ECB53B064AD67274 CRC64;
MWRRLQKLEE QGSQGLPRNK FQKENQQKST NVVYQAHHVS RSKRGQVVGT RGGFRGCTVW
LTGLSGAGKT TVSFALEEYL VSHAIPCYSL DGDNVRHGLN KNLGFSPGDR EENIRRIAEV
AKLFADAGLV CITSFISPFT KDRENARKIH ESAGLPFFEI FVDAPLNICE SRDVKGLYKR
ARAGEIKGFT GIDSDYEKPE TPECVLKTNL TSVSDCVQQV VELLQEQSIV PHTVIKGIHE
LFVPENKLDQ VRAEAESLPS LSITKLDLQW VQILSEGWAT PLKGFMREKE YLQTLHFDTL
LDDGVINMSI PVVLPVSTED KARLEGCGEF ALMYNGRRVA IVRDPEFYEH RKEERCCRVW
GTTSTKHPHI KMVMESGDWL AGGDLQVLQR IRWKDGLDQY RLTPLELKQK CKEMNADAVF
AFQLRNPVHN GHALLMQDTH RRLLERGYKH PVLLLHPLGG WTKDDDVPLD WRMKQHAAVL
EEGVLDPKST IVAIFPSPML YAGPTEVQWH CRCRMMAGAN FYIVGRDPAG MPHPETKKDL
YEPTHGGKVL SMAPGLTSVE IIPFRVAAYN KAKKAMDFYD PERHNEFDFI SGTRMRKLAR
EGENPPDGFM APKAWKVLMD YYRSLEKIN
//
