ID T5HRE1_BACLI Unreviewed; 197 AA.
AC T5HRE1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|HAMAP-Rule:MF_00065};
DE EC=2.7.1.25 {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
GN Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN ORFNames=N399_10055 {ECO:0000313|EMBL:EQM28109.1};
OS Bacillus licheniformis CG-B52.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1368424 {ECO:0000313|EMBL:EQM28109.1, ECO:0000313|Proteomes:UP000017025};
RN [1] {ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|Proteomes:UP000017025};
RA Galvez-Bobadilla E.J., Zarate-Bonilla L.J., Carrillo-Castro K., Guiza L.,
RA Pieper D.H., Salazar M., Junca H.;
RT "Draft genome of a Bacillus sp. strain CG-B52 virulent to shrimps.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQM28109.1, ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|EMBL:EQM28109.1,
RC ECO:0000313|Proteomes:UP000017025};
RX PubMed=27174263;
RA Galvez E.J., Carrillo-Castro K., Zarate L., Guiza L., Pieper D.H.,
RA Garcia-Bonilla E., Salazar M., Junca H.;
RT "Draft Genome Sequence of Bacillus licheniformis CG-B52, a Highly Virulent
RT Bacterium of Pacific White Shrimp (Litopenaeus vannamei), Isolated from a
RT Colombian Caribbean Aquaculture Outbreak.";
RL Genome Announc. 4:0-0(2016).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|ARBA:ARBA00002632, ECO:0000256|HAMAP-Rule:MF_00065,
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|ARBA:ARBA00001823, ECO:0000256|HAMAP-
CC Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000256|ARBA:ARBA00004806, ECO:0000256|HAMAP-
CC Rule:MF_00065, ECO:0000256|RuleBase:RU004347}.
CC -!- SIMILARITY: Belongs to the APS kinase family.
CC {ECO:0000256|ARBA:ARBA00007008, ECO:0000256|HAMAP-Rule:MF_00065,
CC ECO:0000256|RuleBase:RU004347}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQM28109.1}.
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DR EMBL; AVEZ01000029; EQM28109.1; -; Genomic_DNA.
DR RefSeq; WP_003181642.1; NZ_AVEZ01000029.1.
DR AlphaFoldDB; T5HRE1; -.
DR SMR; T5HRE1; -.
DR GeneID; 66216208; -.
DR PATRIC; fig|1368424.3.peg.1484; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000017025; Unassembled WGS sequence.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 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|HAMAP-
KW Rule:MF_00065};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00065}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT ACT_SITE 107
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 197 AA; 22456 MW; 2290C654038F2C2D CRC64;
MVNKDIVWHE ASITKREYHE KNQHKSSIIW LTGLSGSGKS TIANAAAREL FAQGYQVTVL
DGDNVRHGLN KDLGFSDEDR KENIRRIGEV AKLFVEQGTI VITAFISPFK EDRGLVRQLV
EEDEFHEVYV KCDLATCEER DPKGLYKKAR NGEIPFFTGI DSPYEEPETP ELVLDTGAHN
REECKNQLVQ YVKDQTK
//
