ID G2DZQ9_9GAMM Unreviewed; 304 AA.
AC G2DZQ9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ThidrDRAFT_1522 {ECO:0000313|EMBL:EGV32286.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV32286.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV32286.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV32286.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGV32286.1}.
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DR EMBL; AFWT01000008; EGV32286.1; -; Genomic_DNA.
DR RefSeq; WP_007040236.1; NZ_AFWT01000008.1.
DR AlphaFoldDB; G2DZQ9; -.
DR STRING; 765913.ThidrDRAFT_1522; -.
DR PATRIC; fig|765913.3.peg.1545; -.
DR eggNOG; COG0175; Bacteria.
DR OrthoDB; 9772604at2; -.
DR Proteomes; UP000004200; 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 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:EGV32286.1};
KW Transferase {ECO:0000313|EMBL:EGV32286.1}.
FT DOMAIN 33..258
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 280..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 34360 MW; 9992F39E50F8B960 CRC64;
MNRLNTRTLT HLDWLEADAI HILREVVGQC ANPALLFSGG KDSVCLLRLA EKAFRPGPLP
FPLLHIDTGH NYPEVIDFRD RRAAELDARL VVRSVEDSMA RGSVVLKHPS ESRNKHQSVT
LLEAIEEFGF DACIGGARRD EEKSRAKERI MSFRDAFGGW DPKNQRPELW SLYNARVHQG
ENIRAFPISD WTELDVWQYI QREGLALPPI YFAHPRPVVR TKGLLRPVTP LTPALADDQV
EEIRVRFRTV GDITCTAPVE SEADSIDAIL AETAVTTLSE RGATRMDDQT SESSMEERKR
AGYF
//
