ID A0A1M7RDG0_9BURK Unreviewed; 309 AA.
AC A0A1M7RDG0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05192549_12111 {ECO:0000313|EMBL:SHN44240.1};
OS Duganella sacchari.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=551987 {ECO:0000313|EMBL:SHN44240.1, ECO:0000313|Proteomes:UP000184339};
RN [1] {ECO:0000313|EMBL:SHN44240.1, ECO:0000313|Proteomes:UP000184339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sac-22 {ECO:0000313|EMBL:SHN44240.1,
RC ECO:0000313|Proteomes:UP000184339};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC {ECO:0000256|ARBA:ARBA00008885}.
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DR EMBL; FRCX01000021; SHN44240.1; -; Genomic_DNA.
DR RefSeq; WP_072790466.1; NZ_FRCX01000021.1.
DR AlphaFoldDB; A0A1M7RDG0; -.
DR STRING; 551987.SAMN05192549_12111; -.
DR OrthoDB; 9772604at2; -.
DR Proteomes; UP000184339; 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:SHN44240.1};
KW Transferase {ECO:0000313|EMBL:SHN44240.1}.
FT DOMAIN 37..262
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 287..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 34862 MW; E812BA68DA349C08 CRC64;
MNALVEQNAQ VNSRHLDALE SEAIHIMREV AAECSNPALL FSGGKDSVVL LRIAEKAFRP
GKFPFPLVHV DTGHNFQEVI TFRDKRVAEL GERLIVGSVE DSIKKGTVRL RNPQTDSRNA
AQAVTLLETI AEHGFDACIG GARRDEEKAR AKERIFSFRD EFGQWDPKSQ RPELWDLYNT
RVHPGENMRV FPISNWTELD VWQYIAREKL ELPPIYFAHE RQVIPRNGLL VPLTDLTPAR
EGETVETQVV RFRTVGDISC TCPVSSDAAT VEQIIAETAI TQVTERGATR MDDQTSEASM
EKRKKAGYF
//
