ID A0A0Q0UIC3_9CORY Unreviewed; 297 AA.
AC A0A0Q0UIC3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 Name=cysD {ECO:0000313|EMBL:KQB86093.1};
GN ORFNames=Clow_01446 {ECO:0000313|EMBL:KQB86093.1};
OS Corynebacterium lowii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB86093.1, ECO:0000313|Proteomes:UP000050488};
RN [1] {ECO:0000313|EMBL:KQB86093.1, ECO:0000313|Proteomes:UP000050488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB86093.1,
RC ECO:0000313|Proteomes:UP000050488};
RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT human clinical disease and and emended description of Corynebacterium
RT mastiditis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQB86093.1}.
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DR EMBL; LKEV01000004; KQB86093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0UIC3; -.
DR STRING; 1544413.Clow_01446; -.
DR PATRIC; fig|1544413.3.peg.1448; -.
DR Proteomes; UP000050488; 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:KQB86093.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050488};
KW Transferase {ECO:0000313|EMBL:KQB86093.1}.
FT DOMAIN 27..250
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 273..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 33644 MW; 1E229CB9706E5174 CRC64;
MISPHLRDLE DESIHILREV AGQFDKAALL FSGGKDSVVV FELARRAFAP SVVPFELLHV
DTGHNFPEVL AFRDDLVART GARLRVAKVQ DWIDRGDLRE RPDGTRNPLQ TVPLVETIAQ
QGYDAVLGGA RRDEERARAK ERVFSVRDSF GGWDPRRQRP ELWSLYNGAH LPGENIRVFP
ISNWTESDVW EYIGARDIAL PPIYFSHERE VFLRDGMWLT PGEWGGPREG EEIEKRQVRY
RTVGDMSCTG AVESTASSID EVIAEISTST LTERGATRAD DRLSESAMED RKKEGYF
//
