ID A0A1S3UVN7_VIGRR Unreviewed; 306 AA.
AC A0A1S3UVN7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|RuleBase:RU004347};
DE EC=2.7.1.25 {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|RuleBase:RU004347};
GN Name=LOC106769169 {ECO:0000313|RefSeq:XP_014510158.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014510158.1};
RN [1] {ECO:0000313|RefSeq:XP_014510158.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014510158.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|RuleBase:RU004347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000256|RuleBase:RU004347};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000256|RuleBase:RU004347}.
CC -!- SIMILARITY: Belongs to the APS kinase family.
CC {ECO:0000256|RuleBase:RU004347}.
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DR RefSeq; XP_014510158.1; XM_014654672.2.
DR AlphaFoldDB; A0A1S3UVN7; -.
DR GeneID; 106769169; -.
DR KEGG; vra:106769169; -.
DR OrthoDB; 22780at2759; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000087766; 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:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR11055:SF63; ADENYLYL-SULFATE KINASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004347};
KW Kinase {ECO:0000256|RuleBase:RU004347, ECO:0000313|RefSeq:XP_014510158.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004347};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ SEQUENCE 306 AA; 33552 MW; 634C0BDBFDB4F25A CRC64;
MITAKAPPPP YTSGFFRKIE SGPSPAVETL GLAKLRGINV GGLYRSRRSF VAHARSKPIK
AKENTGASLI DDWFKPIQAK DDSDIEECAT AFPGKNLPQM SNVGNSTNIL WHDCPIQKQD
RQQLLQQKGC VIWLTGLSGS GKSTIACALS RSLHSRGKLS YILDGDNIRH GLNHDLSFRA
EDRSENIRRI GEVAKLFADA GVICITSLIS PYQKDRDACR ALLPKGDFIE VFIDVPLQVC
EARDPKGLYK LARAGKIKGF TGIDDPYEPP CSCEIVLQQK GSGCKSPSDM AEIVISYLEE
NGYLRA
//
