ID A0A3A1U1U3_9MICO Unreviewed; 171 AA.
AC A0A3A1U1U3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|RuleBase:RU004347};
DE EC=2.7.1.25 {ECO:0000256|RuleBase:RU004347};
GN Name=cysC {ECO:0000313|EMBL:RIX28905.1};
GN ORFNames=D1781_11250 {ECO:0000313|EMBL:RIX28905.1};
OS Amnibacterium setariae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Amnibacterium.
OX NCBI_TaxID=2306585 {ECO:0000313|EMBL:RIX28905.1, ECO:0000313|Proteomes:UP000265742};
RN [1] {ECO:0000313|Proteomes:UP000265742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD4a {ECO:0000313|Proteomes:UP000265742};
RA Kim I.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RIX28905.1}.
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DR EMBL; QXTG01000002; RIX28905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1U1U3; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000265742; 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: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 InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 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|RuleBase:RU004347};
KW Kinase {ECO:0000256|RuleBase:RU004347, ECO:0000313|EMBL:RIX28905.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004347};
KW Reference proteome {ECO:0000313|Proteomes:UP000265742};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ SEQUENCE 171 AA; 17532 MW; AABA8107CF7D79B6 CRC64;
MLFTGLSGAG KSTIARAVAA RLLEQGDLVS VLDGDEVRQV LSAGLGFDAE DRARNVARIA
WVAAEIARVG GTAIAAPIAP FAAGRAQARR RAEAAGARFL LVHVATPLAV CEARDRKGLY
AAAREGRLPD FTGVSSPYEA PLDADVTVDA AVAAVDEAAD AVVAALAAVR R
//