ID G3P3K0_GASAC Unreviewed; 625 AA.
AC G3P3K0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=3'-phosphoadenosine 5'-phosphosulfate synthase 2a {ECO:0000313|Ensembl:ENSGACP00000012173.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000012173.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000012173.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000012173.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; G3P3K0; -.
DR STRING; 69293.ENSGACP00000012173; -.
DR Ensembl; ENSGACT00000012197.1; ENSGACP00000012173.1; ENSGACG00000009195.1.
DR eggNOG; KOG4238; Eukaryota.
DR GeneTree; ENSGT00390000009613; -.
DR InParanoid; G3P3K0; -.
DR OMA; TENCTPE; -.
DR TreeFam; TF313143; -.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000009195; Expressed in intestinal epithelial cell and 11 other cell types or tissues.
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: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:UP000007635};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 234..387
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 395..618
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 625 AA; 70277 MW; 694EA211EC7F5C8C CRC64;
LQRPPFLCMR AFLYHNYGSC QDLNRSTNVV YQAHHVSRSK RGQVVGTRGG FRGCTIWLTG
LSGAGKTTIS FALEEFLVSH AIPCYSLDGD NIRHGLNKNL GFSAVDREEN IRRIAEVAKL
FADAGLVCVT SFISPFGKDR DEARKIHASA GLPFFEVFIH ASLAVCEKRD VKGLYKKARA
GEIKGFTGID SDYERPEAPD LVLKTGELSV NECLHQVLEL LKEQNIVPGE IMEEVNELFV
MENKLNLAVA DANTLPTISI TKLDLQWVQV LSEGWASPLK GFMREREFLQ VLHFGNLLDG
GAINLSVPIV LPVSNETKQE VDGCAAVALE YQGSRVAILR NPEFYQHRKE ERCARQWGTT
CPQHPYIKMV MEGGDWLVGG DLEVLERIQW NDGLDQYRLT PQELKQKFKD MEADAVFAFQ
LRNPVHNGHA LLMQDTKRRL LERGYKNPVL LLHPLGGWTK DDDVPLDWRM KQHAAVLEEG
VLEPASTIVA IFPSPMMYAG PTEVQWHCRA RMIAGANFYI VGRDPAGMPH PETKQDLYEP
THGAKVLTMA PGLTSVEIIP FRVAAYNKVK KAMDFYEAER HAEFEFISGT KMRNMARSGE
NPPDGFMAPK AWKVLVEYYT SLQKD
//
