ID A0A1M3BV10_9BACT Unreviewed; 356 AA.
AC A0A1M3BV10;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=BGO17_04235 {ECO:0000313|EMBL:OJU88149.1};
OS Candidatus Saccharibacteria bacterium 49-20.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1895829 {ECO:0000313|EMBL:OJU88149.1, ECO:0000313|Proteomes:UP000184370};
RN [1] {ECO:0000313|EMBL:OJU88149.1, ECO:0000313|Proteomes:UP000184370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=49-20 {ECO:0000313|EMBL:OJU88149.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJU88149.1}.
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DR EMBL; MKSN01000001; OJU88149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3BV10; -.
DR STRING; 1895829.BGO17_04235; -.
DR Proteomes; UP000184370; 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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
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}.
FT DOMAIN 9..248
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 356 AA; 38685 MW; DF87F35DEB8993E9 CRC64;
MNLLEHESKQ LLSASQIPVP LGKILTKDQV QEVSLPAVLK SQVPTGGRGK AGGILIIDTQ
EKLEEAAKKL FNLEIKGHLP QVLLAEEKLA IARELYLSLL IDRKTSSLKL IAHTNGGVEV
EENKDFASWL VDYSKPDINT LGQALAEYFI LEDKTFVLQD LIENLITCFK QNDATLIEIN
PLVVTEDGKI IAGDCKMTLD DAAAFRHPEW NFEAKTAEVN FVTINPEGNV ATIANGAGLA
MATVDAAYDA GLIPANFLDI GGGANTESLL KAFNKIIEYP NVQAIILNVF AGITRADEVA
RAIVEAQKSI SNLPPLFIRL TGTNSDEAKE ILEKNQIQML PNLESCLKAA KESIDA
//