ID B8FTM8_DESHD Unreviewed; 598 AA.
AC B8FTM8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=sulfate adenylyltransferase {ECO:0000256|ARBA:ARBA00012391};
DE EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391};
GN OrderedLocusNames=Dhaf_4111 {ECO:0000313|EMBL:ACL22120.1};
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL22120.1, ECO:0000313|Proteomes:UP000007726};
RN [1] {ECO:0000313|EMBL:ACL22120.1, ECO:0000313|Proteomes:UP000007726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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DR EMBL; CP001336; ACL22120.1; -; Genomic_DNA.
DR RefSeq; WP_015945027.1; NC_011830.1.
DR AlphaFoldDB; B8FTM8; -.
DR KEGG; dhd:Dhaf_4111; -.
DR HOGENOM; CLU_007265_5_3_9; -.
DR Proteomes; UP000007726; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:InterPro.
DR CDD; cd04166; CysN_ATPS; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR041757; CysN_GTP-bd.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR NCBIfam; TIGR02034; CysN; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ACL22120.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACL22120.1}.
FT DOMAIN 4..218
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 598 AA; 67127 MW; 0289EED5953217A6 CRC64;
MDNREQMNIV IVGHVDHGKS TVIGRLLADT GSLPEGKLEA VQEYCRKNAR PFEYAFLLDA
LKDEQAQGIT IDTARSFFKT GKRDYIIIDA PGHIEFLKNM VTGASRAEAA LLVIDAKEGI
RENSKRHGHI AAMLGIRQVV VLVNKMDLVD FDRQTFETIR REFGEFLHKL NIQPVNFIPL
SAFNGDNIAV RSQRTAWYEG PTVLEQLDSL SNRKGNQELP LRMPVQDIYK FTAAGDDRRI
VAGTILSGTI RSGDEVVFLP SRKRSVIQSI EGFNVSQRNM AYADEAVGLT LKTQIYIKPG
ELMVKAQDKQ PQMGSRFKAN IFWVGKAPLI KNKTYKLKIG TLKIGVKMVE ILNIIDAAEL
NIDTFKDQAE KHDVAECIFE TAKPIAFDPV TEMEQTGRFV IVDNYEISGG GIILEQVDDD
RSSLQEHVRQ RETQWEKGLI QPAQRAGIYG HKAKFIVLTS GSADHGPVIE TIARELEQTL
FRLNYKAYYL GVRNLLHGLA AEETIKDWSR DREIRQVGEL ARILTDSGQI FITTVFNLED
DEAENLKLLN QPSEILVITI GESPFYSFQP DASLEVEGAV AAVGGLLQKQ EIILDYYL
//
