ID A0A2Y9EFL1_PHYMC Unreviewed; 603 AA.
AC A0A2Y9EFL1; A0A2Y9S8Y3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 isoform X2 {ECO:0000313|RefSeq:XP_007100643.2, ECO:0000313|RefSeq:XP_007100644.2};
GN Name=PAPSS1 {ECO:0000313|RefSeq:XP_007100643.2,
GN ECO:0000313|RefSeq:XP_007100644.2, ECO:0000313|RefSeq:XP_007100646.2,
GN ECO:0000313|RefSeq:XP_023975116.2, ECO:0000313|RefSeq:XP_023975117.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007100646.2};
RN [1] {ECO:0000313|RefSeq:XP_007100643.2, ECO:0000313|RefSeq:XP_007100644.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007100643.2,
RC ECO:0000313|RefSeq:XP_007100644.2};
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_007100643.2; XM_007100581.4.
DR RefSeq; XP_007100644.2; XM_007100582.4.
DR RefSeq; XP_007100646.2; XM_007100584.4.
DR RefSeq; XP_023975116.2; XM_024119348.3.
DR RefSeq; XP_023975117.1; XM_024119349.3.
DR STRING; 9755.ENSPCTP00005001538; -.
DR Ensembl; ENSPCTT00005001691; ENSPCTP00005001538; ENSPCTG00005001117.
DR KEGG; pcad:102993360; -.
DR OrthoDB; 22780at2759; -.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000248484; Chromosome 7.
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:SF17; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE 1; 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:UP000248484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 212..364
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 373..596
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 603 AA; 68409 MW; 066EC4317B4A00B5 CRC64;
MQRATNVTYQ AHHVSRNKRG QVVGTRGGSR GCTVWLTGLS GAGKTTVSMA LEEYLVCHGI
PCYTLDGDNI RQGLNKNLGF SPEDREENVR RIAEVAKLFA DAGLVCITSF ISPYTQDRNN
ARQIHEGASL PFFEVFVDAP LHVCEQRDVK GLYKKARAGE IKGFTGIDSE YEKPEAPELV
LKTDSCDVND CVQQVVELLQ ERDIVPVDAS YEVKELYVPE NKLHLAKTDA ETLPALKINK
VDMQWVQVLA EGWATPLNGF MREREYLQCL HFDCLLDGGV INLSVPIVLT ATQEDKERLD
GCTAFALMYE GRRVAILRNP EFFEHRKEER CARQWGTTCK NHPYIKMVME QGDWLIGGDL
QVLDRIYWND GLDQYRFTPS ELKQKFKDMN ADAVFAFQLR NPVHNGHALL MQDTHKQLLE
RGYRRPVLLL HPLGGWTKDD DVPLMWRMKQ HAAVLEEGVL NPETTVVAIF PSPMMYAGPT
EVQWHCRARM VAGANFYIVG RDPAGVPHPE TGEGLYEPTH GAKVLTMAPG LITLEIVPFR
VAAYNKKKKQ MDYYDAEHHE DFEFISGTRM RKLAREGQKP PEGFMAPKAW TVLMEYYKSL
EKA
//
