ID D6GWH3_PARA5 Unreviewed; 366 AA.
AC D6GWH3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Succinate--CoA ligase (ADP-forming) {ECO:0000313|EMBL:EFD92436.1};
GN ORFNames=BJBARM5_0850 {ECO:0000313|EMBL:EFD92436.1};
OS Candidatus Parvarchaeum acidophilus ARMAN-5.
OC Archaea; Candidatus Parvarchaeota; Parvarchaeum.
OX NCBI_TaxID=662762 {ECO:0000313|EMBL:EFD92436.1, ECO:0000313|Proteomes:UP000009376};
RN [1] {ECO:0000313|EMBL:EFD92436.1, ECO:0000313|Proteomes:UP000009376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20421484; DOI=10.1073/pnas.0914470107;
RA Baker B.J., Comolli L.R., Dick G.J., Hauser L.J., Hyatt D., Dill B.D.,
RA Land M.L., Verberkmoes N.C., Hettich R.L., Banfield J.F.;
RT "Enigmatic, ultrasmall, uncultivated Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8806-8811(2010).
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DR EMBL; GG745596; EFD92436.1; -; Genomic_DNA.
DR AlphaFoldDB; D6GWH3; -.
DR Proteomes; UP000009376; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EFD92436.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000009376}.
FT DOMAIN 10..232
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 366 AA; 40196 MW; E7D89A262BE52377 CRC64;
MVDLLEHEGK KIFKSYGISI PSGYIIHSFK EVKKPEKECV VKAQVPSGHR GINGGVVKVK
EKEEILKAIN KISSINFNGF KATSFLVEEM VPHTKEVYVG LTLDRSRKMP VLILSPSGGV
DIEHVPANQI KKFYLDILLG MQNYIKREAF NFIGLSENYR EIFYTLMERL WNVFTGEDCE
LVEINPLAVT SSGLVALDSK VTIEDDALFR HKNYQKEYTS LDPLEAEAKR KDIAFVRLGG
DIGLIANGAG LTLATIDQIK LAGGSAGDFL DLGGTDDPEK VAEAINLVKK AKPKVVFINI
FGGVTKADTV AEGIIKAIKD SDTNPKIIVR LMGVNNQRGI QLLKANGIDA FTDISEAVKK
AVEVSN
//
