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Database: UniProt
Entry: A0A120A3M3_BACSE
LinkDB: A0A120A3M3_BACSE
Original site: A0A120A3M3_BACSE 
ID   A0A120A3M3_BACSE        Unreviewed;       303 AA.
AC   A0A120A3M3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00064};
DE            EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00064};
DE   AltName: Full=ATP-sulfurylase small subunit {ECO:0000256|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00064};
DE            Short=SAT {ECO:0000256|HAMAP-Rule:MF_00064};
GN   Name=cysD {ECO:0000256|HAMAP-Rule:MF_00064,
GN   ECO:0000313|EMBL:KWR57011.1};
GN   ORFNames=AA415_00467 {ECO:0000313|EMBL:KWR57011.1}, DW668_06720
GN   {ECO:0000313|EMBL:RHF76275.1}, DW853_05585
GN   {ECO:0000313|EMBL:RHC32119.1}, DW889_12465
GN   {ECO:0000313|EMBL:RHB26995.1}, DWV41_06880
GN   {ECO:0000313|EMBL:RGW98140.1}, DWV77_07910
GN   {ECO:0000313|EMBL:RGW34246.1}, DWY58_04870
GN   {ECO:0000313|EMBL:RGR29356.1}, DWY65_10960
GN   {ECO:0000313|EMBL:RGR12157.1}, DWZ78_07620
GN   {ECO:0000313|EMBL:RHM19164.1}, DXC34_04030
GN   {ECO:0000313|EMBL:RGM15042.1}, F9950_14925
GN   {ECO:0000313|EMBL:KAB5325200.1}, F9958_15130
GN   {ECO:0000313|EMBL:KAB5310672.1}, F9962_17050
GN   {ECO:0000313|EMBL:KAB5279024.1};
OS   Bacteroides stercoris.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=46506 {ECO:0000313|EMBL:KWR57011.1, ECO:0000313|Proteomes:UP000056419};
RN   [1] {ECO:0000313|EMBL:KWR57011.1, ECO:0000313|Proteomes:UP000056419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR57011.1,
RC   ECO:0000313|Proteomes:UP000056419};
RX   PubMed=26768901; DOI=10.1186/s12864-016-2377-z;
RA   Coyne M.J., Roelofs K.G., Comstock L.E.;
RT   "Type VI secretion systems of human gut Bacteroidales segregate into three
RT   genetic architectures, two of which are contained on mobile genetic
RT   elements.";
RL   BMC Genomics 17:58-58(2016).
RN   [2] {ECO:0000313|EMBL:KWR57011.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR57011.1};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000261223, ECO:0000313|Proteomes:UP000283310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF05-4 {ECO:0000313|EMBL:RGW98140.1,
RC   ECO:0000313|Proteomes:UP000284777}, AF12-7
RC   {ECO:0000313|EMBL:RGW34246.1, ECO:0000313|Proteomes:UP000285150},
RC   AF25-6 {ECO:0000313|EMBL:RGR29356.1,
RC   ECO:0000313|Proteomes:UP000284161}, AF26-20BH
RC   {ECO:0000313|EMBL:RGR12157.1, ECO:0000313|Proteomes:UP000283310},
RC   AF35-20 {ECO:0000313|EMBL:RHM19164.1,
RC   ECO:0000313|Proteomes:UP000284604}, AM25-16
RC   {ECO:0000313|EMBL:RHF76275.1, ECO:0000313|Proteomes:UP000283762},
RC   AM36-9BH {ECO:0000313|EMBL:RHC32119.1,
RC   ECO:0000313|Proteomes:UP000285305}, AM40-34
RC   {ECO:0000313|EMBL:RHB26995.1, ECO:0000313|Proteomes:UP000283482}, and
RC   TF03-6 {ECO:0000313|EMBL:RGM15042.1,
RC   ECO:0000313|Proteomes:UP000261223};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000431177, ECO:0000313|Proteomes:UP000440773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A17 {ECO:0000313|EMBL:KAB5279024.1,
RC   ECO:0000313|Proteomes:UP000440773}, BIOML-A2
RC   {ECO:0000313|EMBL:KAB5325200.1, ECO:0000313|Proteomes:UP000431177},
RC   and BIOML-A6 {ECO:0000313|EMBL:KAB5310672.1,
RC   ECO:0000313|Proteomes:UP000467334};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
CC   -!- FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the
CC       adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC       diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC       APS synthesis involves the formation of a high-energy phosphoric-
CC       sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC       to ATP hydrolysis by CysD. {ECO:0000256|HAMAP-Rule:MF_00064}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00064};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00064}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC       {ECO:0000256|HAMAP-Rule:MF_00064}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008885, ECO:0000256|HAMAP-Rule:MF_00064}.
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:KWR57011.1}.
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DR   EMBL; WCLP01000066; KAB5279024.1; -; Genomic_DNA.
DR   EMBL; WCLE01000043; KAB5310672.1; -; Genomic_DNA.
DR   EMBL; WCLA01000038; KAB5325200.1; -; Genomic_DNA.
DR   EMBL; LRGC01000002; KWR57011.1; -; Genomic_DNA.
DR   EMBL; QSSV01000004; RGM15042.1; -; Genomic_DNA.
DR   EMBL; QRTW01000018; RGR12157.1; -; Genomic_DNA.
DR   EMBL; QRUB01000002; RGR29356.1; -; Genomic_DNA.
DR   EMBL; QSAF01000007; RGW34246.1; -; Genomic_DNA.
DR   EMBL; QSBD01000007; RGW98140.1; -; Genomic_DNA.
DR   EMBL; QSGN01000033; RHB26995.1; -; Genomic_DNA.
DR   EMBL; QSHQ01000007; RHC32119.1; -; Genomic_DNA.
DR   EMBL; QRHJ01000014; RHF76275.1; -; Genomic_DNA.
DR   EMBL; QRPN01000006; RHM19164.1; -; Genomic_DNA.
DR   RefSeq; WP_005654990.1; NZ_WCLU01000065.1.
DR   AlphaFoldDB; A0A120A3M3; -.
DR   STRING; 46506.AA415_00467; -.
DR   GeneID; 31797233; -.
DR   PATRIC; fig|46506.5.peg.503; -.
DR   OMA; LMIDTGH; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000056419; Unassembled WGS sequence.
DR   Proteomes; UP000261223; Unassembled WGS sequence.
DR   Proteomes; UP000283310; Unassembled WGS sequence.
DR   Proteomes; UP000283482; Unassembled WGS sequence.
DR   Proteomes; UP000283762; Unassembled WGS sequence.
DR   Proteomes; UP000284161; Unassembled WGS sequence.
DR   Proteomes; UP000284604; Unassembled WGS sequence.
DR   Proteomes; UP000284777; Unassembled WGS sequence.
DR   Proteomes; UP000285150; Unassembled WGS sequence.
DR   Proteomes; UP000285305; Unassembled WGS sequence.
DR   Proteomes; UP000431177; Unassembled WGS sequence.
DR   Proteomes; UP000440773; Unassembled WGS sequence.
DR   Proteomes; UP000467334; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00064; Sulf_adenylyltr_sub2; 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   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00064};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00064};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00064,
KW   ECO:0000313|EMBL:KWR57011.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000056419};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:KWR57011.1}.
FT   DOMAIN          30..257
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
SQ   SEQUENCE   303 AA;  35720 MW;  B6097FD28FEE7C13 CRC64;
     MKEEYKLSHL KELEAESIHI IREVAAEFEN PVMLYSIGKD SSVMVRLAEK AFAPGKVPFP
     LMHIDSKWKF KEMIQFRDEY ARKYGWNLIV ESNMEAFEAG VGPFTHGSKV HTDLMKTQAL
     LHALDKYKFD AAFGGARRDE EKSRAKERIF SFRDKFHQWD PKNQRPELWD IYNARVHKGE
     SIRVFPLSNW TELDIWQYIR LENIPIVPLY FAKERPCVEI DGNLIMADDD RLPEQYREKI
     EMRMVRFRTL GCWPLTGAVE SSADTIEKIV EEMMTTTKSE RTTRVIDFDQ EASMEQKKRE
     GYF
//
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