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Entry: U2KS18_9FIRM
LinkDB: U2KS18_9FIRM
Original site: U2KS18_9FIRM 
ID   U2KS18_9FIRM            Unreviewed;       299 AA.
AC   U2KS18;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   ORFNames=RUMCAL_01842 {ECO:0000313|EMBL:ERJ94885.1};
OS   Ruminococcus callidus ATCC 27760.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ94885.1, ECO:0000313|Proteomes:UP000016662};
RN   [1] {ECO:0000313|EMBL:ERJ94885.1, ECO:0000313|Proteomes:UP000016662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ94885.1,
RC   ECO:0000313|Proteomes:UP000016662};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:ERJ94885.1}.
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DR   EMBL; AWVF01000232; ERJ94885.1; -; Genomic_DNA.
DR   RefSeq; WP_021683340.1; NZ_KI260480.1.
DR   AlphaFoldDB; U2KS18; -.
DR   STRING; 411473.RUMCAL_01842; -.
DR   GeneID; 78476275; -.
DR   PATRIC; fig|411473.3.peg.1509; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_9; -.
DR   OrthoDB; 9772604at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000016662; 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:ERJ94885.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:ERJ94885.1}.
FT   DOMAIN          28..253
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          277..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   299 AA;  34665 MW;  4518C5D4D549828F CRC64;
     MHELSHLDEL EAEAIYIIRE VAAECEKPVM LYSIGKDSSV MLHLAMKAFY PEKPPFPFLH
     IDTTWKFKDM IRFRDETAKK LGIEMLVYTN EEGVKQGINP FDHGAAYTDI MKTQALKQAL
     TKYGFTAAFG GGRRDEEKSR AKERIFSFRN EAQAWDPKNQ RPEMWKLYNT KIKKGESMRV
     FPISNWTEKD IWQYIKRENI DIVPLYFAAE RPVVYRDGNI IMVDDDRLPL KPGEKPEYKS
     IRFRTLGCYP LTGGIESTAT TLDEIIDETL SSVSSERTSR VIDNEAAGSM ERRKREGYF
//
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