ID A0A093RR00_PYGAD Unreviewed; 601 AA.
AC A0A093RR00;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 {ECO:0000313|EMBL:KFW73269.1};
DE Flags: Fragment;
GN ORFNames=AS28_02332 {ECO:0000313|EMBL:KFW73269.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW73269.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW73269.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW73269.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL225529; KFW73269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093RR00; -.
DR STRING; 9238.A0A093RR00; -.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000054081; 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: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:UP000054081};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 209..361
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 370..593
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW73269.1"
FT NON_TER 601
FT /evidence="ECO:0000313|EMBL:KFW73269.1"
SQ SEQUENCE 601 AA; 67357 MW; C1C6A86341D73676 CRC64;
STNVVYQAHH VSRSKRGQVV GTRGGFRGCT VWLTGLSGAG KTTIGFALEE YLVAHGIPCY
SLDGDNVRHG LNKNLGFSAG DREENIRRIA EVARLFADAG LVCITSFISP FAKDRQNARK
IHEAAGLPFF EIFVDAPLNI CESRDVKGLY KKARAGEIKG FTGIDSEYEK PESPELVLKT
NVASVSECIQ QVVELLQTQT IVPPGSIKDV LELFVPENKL NSVRAEAEML PSVEITKLDL
QWVQVLSEGW ATPLTGFMRE AEYLQVIHFG TLLNDGVVNL SIPIVLPIST EDKERLEGCE
ALALSYAGRR VAVLKSPEYF EHRKEERCAR IWGTTCTKHP HIKMVMESGD WLVGGDLLVL
EKIKWNDGLD QYRLTPLGLK QKFAEMNADA VFAFQLRNPV HNGHALLMQD TRRQLLERGY
KNPVLLLHPL GGWTKDDDVP LEWRMKQHAA VLEEQVLDPK STIVAIFPSP MLYAGPTEVQ
WHCRARMIAG ANFYIVGRDP AGMPHPETKK DLYEPTQGGK VLSMAPGLTS VEIIPFRVAA
YNKLKRAMDF YDPKRHDDFD FISGTRMRKL AREGENPPDG FMAPKAWKVL TEYYQSLEKK
N
//
