ID A0A0P7YPK1_9SPHN Unreviewed; 300 AA.
AC A0A0P7YPK1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Sulfate adenylyltransferase subunit 2 {ECO:0000256|ARBA:ARBA00022004};
DE EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391};
DE AltName: Full=ATP-sulfurylase small subunit {ECO:0000256|ARBA:ARBA00030256};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|ARBA:ARBA00031812};
GN ORFNames=HLUCCX21_02510 {ECO:0000313|EMBL:KPQ32308.1};
OS Porphyrobacter sp. HL-46.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1479239 {ECO:0000313|EMBL:KPQ32308.1, ECO:0000313|Proteomes:UP000054043};
RN [1] {ECO:0000313|EMBL:KPQ32308.1, ECO:0000313|Proteomes:UP000054043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-46 {ECO:0000313|EMBL:KPQ32308.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000262};
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC {ECO:0000256|ARBA:ARBA00008885}.
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:KPQ32308.1}.
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DR EMBL; LLEX01000086; KPQ32308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7YPK1; -.
DR STRING; 1479239.GCA_000744895_01691; -.
DR PATRIC; fig|1479239.6.peg.492; -.
DR eggNOG; COG0175; Bacteria.
DR OrthoDB; 9772604at2; -.
DR Proteomes; UP000054043; Unassembled WGS sequence.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR NCBIfam; TIGR02039; CysD; 1.
DR PANTHER; PTHR43196; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR PANTHER; PTHR43196:SF1; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF002936; CysDAde_trans; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000313|EMBL:KPQ32308.1};
KW Transferase {ECO:0000313|EMBL:KPQ32308.1}.
FT DOMAIN 27..254
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 278..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 34112 MW; B12D3FAEEC9C690C CRC64;
MRNLTHLERL EAESIHIFRE VVAEAENPVM LYSVGKDSSV MLHLARKAFY PAPPPFPMLH
VASGWDFQDL IVHRDHTVSE YGLRLIIAQN EEAEAQGINP FDTGSALYSQ AQLTDPLKRA
LTAHGFDAAF GGGRRDEEKA RAKERIFSFR TAAHRWDPKN QRPELWNLYN AKKSKGESIR
VFPISNWTEL DIWQYIALEN IDIVPLYFSK PRLTVERDGM ILVVDDDRFR LEPGEAPVMR
PVRFRTLGCY PLTGATVSTA ADMNTIIQEM LLATSSERQG RAIDKGQSAS MEDKKQEGYF
//
