ID A0A1X1V6F1_9MYCO Unreviewed; 309 AA.
AC A0A1X1V6F1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=AWC06_06455 {ECO:0000313|EMBL:ORV64696.1};
OS Mycobacterium fragae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1260918 {ECO:0000313|EMBL:ORV64696.1, ECO:0000313|Proteomes:UP000194000};
RN [1] {ECO:0000313|EMBL:ORV64696.1, ECO:0000313|Proteomes:UP000194000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45731 {ECO:0000313|EMBL:ORV64696.1,
RC ECO:0000313|Proteomes:UP000194000};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) 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:ORV64696.1}.
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DR EMBL; LQOW01000003; ORV64696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1V6F1; -.
DR STRING; 1260918.AWC06_06455; -.
DR OrthoDB; 9772604at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000194000; 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:ORV64696.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194000};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:ORV64696.1}.
FT DOMAIN 40..262
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 309 AA; 35028 MW; 6A1C4019087DC814 CRC64;
MTSQVTAGPA AGQYELSHLR SLEAEAIHII REVAAEFERP VLLFSGGKDS IVMLHLALKA
FRPGRLPFPV MHVDTGHNFD EVLETRDQLV AETGVRLIVA KVQDDIDAGR VVETIPSRNP
IQTVTLLRAI RENKFDAAFG GARRDEEKAR AKERVFSFRD EFGQWDPKAQ RPEVWNLYNG
RHHKGEHIRV FPLSNWTEFD VWSYIGAEKI TLPSIYYAHR RKVFERDGML LAVHRHMQPR
PDEKVFEATV RFRTVGDVTC TGCVESTAAT AAEVIAETAV SRLTERGATR ADDRISEAGM
EDRKRQGYF
//
