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Database: UniProt
Entry: A0A1J5IF16_9GAMM
LinkDB: A0A1J5IF16_9GAMM
Original site: A0A1J5IF16_9GAMM 
ID   A0A1J5IF16_9GAMM        Unreviewed;       283 AA.
AC   A0A1J5IF16;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=AUK56_04600 {ECO:0000313|EMBL:OIP95661.1};
OS   Thiomicrospira sp. CG2_30_44_34.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=1805397 {ECO:0000313|EMBL:OIP95661.1, ECO:0000313|Proteomes:UP000182935};
RN   [1] {ECO:0000313|EMBL:OIP95661.1, ECO:0000313|Proteomes:UP000182935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_44_34 {ECO:0000313|EMBL:OIP95661.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIP95661.1}.
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DR   EMBL; MNZS01000037; OIP95661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5IF16; -.
DR   STRING; 1805397.AUK56_04600; -.
DR   Proteomes; UP000182935; 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:OIP95661.1};
KW   Transferase {ECO:0000313|EMBL:OIP95661.1}.
FT   DOMAIN          11..237
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
SQ   SEQUENCE   283 AA;  33252 MW;  8EE458D1AC454BEB CRC64;
     MREVVAEFEN PAMLYSIGKD SSVMLHLAQK AFYPAPPPFP LVHVDTTWKF KEMIEFRDKR
     AKEVGMELIV HTNPKGAELN ISPFEHGSTM HTDMMKTEGL RQMLDYYQYD AVFGGARRDE
     EKSRAKERIY SFRDEHHRWD PKNQRPELWD IYNGRHKKGE SIRIFPLSNW TELDIWQYIY
     LEKVPIPDLY FAKERPVVEY GGTKIMVDDD RMPEALRKTA KMEKVRFRTL GCYPLTGAVE
     SEATTLPEII QEMLLTKVSE RQGRMIDHDE AGSMEKKKME GYF
//
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