ID A4G7P0_HERAR Unreviewed; 443 AA.
AC A4G7P0;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=sulfate adenylyltransferase {ECO:0000256|ARBA:ARBA00012391};
DE EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391};
GN Name=cysN {ECO:0000313|EMBL:CAL62527.1};
GN OrderedLocusNames=HEAR2396 {ECO:0000313|EMBL:CAL62527.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL62527.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL62527.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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DR EMBL; CU207211; CAL62527.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G7P0; -.
DR STRING; 204773.HEAR2396; -.
DR KEGG; har:HEAR2396; -.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_2_4; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000006697; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd03695; CysN_NodQ_II; 1.
DR CDD; cd04095; CysN_NoDQ_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR041757; CysN_GTP-bd.
DR InterPro; IPR044138; CysN_II.
DR InterPro; IPR044139; CysN_NoDQ_III.
DR InterPro; IPR004161; EFTu-like_2.
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; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:CAL62527.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAL62527.1}.
FT DOMAIN 20..244
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 443 AA; 48730 MW; 96E770AE6ADF7EB3 CRC64;
MNAVLAEQAI TRTGGNAAER GLLRFITAGS VDDGKSTLIG RLLFDSKGIF ADQLDAMSRA
KHKRTVGDTI DLSLLTDGLE AEREQGITID VAYRYFATPK RKFIIADTPG HEQYTRNMVT
GASTADAVII LIDVSKVKLG DDGSVELLIQ TKRHSTIAHL LQIEHVIVAV NKMDLVNYDQ
KVYDRIVAAY VEFAKTLGLK DIHPIPLSAL AGDNVVTRGD KLGWYQGPTL IELLESLSVY
DESHDEPFRF PVQLVARHNG HEADDFRGYM GRIEAGKVRK GDKLVVQPSG QTATVKDIQT
FDGSIEQAVV GQSITLLLEE HVDISRGDML SAADRPAELL KTVHADLCWL SEEPLDLRRK
YWLKHTTRQV GARVTKIESL LDINTQEKRA ADEVKLNGIA SVTINVQQPL AADAYDAIRS
TGAFILIDEV THQTVAAGMI RLA
//
