ID A0A1S3N3T3_SALSA Unreviewed; 614 AA.
AC A0A1S3N3T3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2-like {ECO:0000313|RefSeq:XP_014010119.1};
GN Name=LOC106577008 {ECO:0000313|RefSeq:XP_014010119.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014010119.1};
RN [1] {ECO:0000313|RefSeq:XP_014010119.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014010119.1};
RG RefSeq;
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 RefSeq; XP_014010119.1; XM_014154644.1.
DR AlphaFoldDB; A0A1S3N3T3; -.
DR STRING; 8030.ENSSSAP00000112829; -.
DR PaxDb; 8030-ENSSSAP00000112829; -.
DR Ensembl; ENSSSAT00000147836; ENSSSAP00000112808; ENSSSAG00000078725.
DR GeneID; 106577008; -.
DR KEGG; sasa:106577008; -.
DR OrthoDB; 22780at2759; -.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000087266; Chromosome ssa18.
DR Bgee; ENSSSAG00000078725; Expressed in mesonephros and 10 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:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 221..375
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 383..606
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 614 AA; 69367 MW; 4B1A6A1AB4879119 CRC64;
MLGVKTQQTD LNRSTNVVFQ AHHVTRSKRG QVVGTRGGFR GCTVWLTGLS GAGKTTIAFA
LEEYLVSHGI PCYSLDGDNI RHGLNKNLGF TATDREENIR RIAEVAKLFA DAGLVCITSF
ISPYTKDRDD ARKILESAGL PFFEVFINAP LEVCESRDVK GLYKKARAGE IKGFTGIDAE
YERPEAPELV LKTGEITVTE CIRQVVDLLR EQSIVPSGIT EEVNELFVPE NKLKLVQVDA
ITLPTISITK LDLQWVQVLA EGWATPLKGF MREREFLQVQ HFGNLLDDGT INQSIPIVLP
VTTETKQRLD GCAAVALEFQ GTLVAILRQP EFYEHRKEER CARQWGTTCP QHPYIKMVME
GGDWLVGGDL EVLERIRWND GLDQYRFTPR ELKQKFKEMK ADAIFAFQLR NPVHNGHALL
MQDTKRRLLE RGYKRPVLLL HPLGGWTKDD DVPLDWRMKQ HTAVLEEGVL DPTSTIVAIF
PSPMMYAGPT EVQWHCRARM IAGANFYIVG RDPAGMPHPE TKQDIYEPTH GGKVLTMAPG
LTSVEIIPFR VAAYNKTKRA MDFYDKDRHA EFEFISGTRM RKLARCGENP PDGFMAPKAW
KVLTEYYSSI QKDQ
//
