ID   A0A218QHT0_9CYAN        Unreviewed;       428 AA.
AC   A0A218QHT0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|EMBL:GAX41448.1};
GN   ORFNames=NIES4075_24180 {ECO:0000313|EMBL:GAX41448.1};
OS   Tolypothrix sp. NIES-4075.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX41448.1, ECO:0000313|Proteomes:UP000198313};
RN   [1] {ECO:0000313|EMBL:GAX41448.1, ECO:0000313|Proteomes:UP000198313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX41448.1,
RC   ECO:0000313|Proteomes:UP000198313};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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:GAX41448.1}.
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DR   EMBL; BDUC01000002; GAX41448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218QHT0; -.
DR   Proteomes; UP000198313; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 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   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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000198313}.
FT   DOMAIN          30..232
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   428 AA;  47452 MW;  9BEF18FE49662DC9 CRC64;
     MRAIHLQRRH FLEVAIQGAY FMDLLEYQVK EWFGNIGIPV LPSQRIDHPT DLKRLKIRYP
     IVLKSQVHAQ ERAKAGGVRF VETTIDAIAA AQNIFNLPIL GELPEVLLAE SKYDADQEYY
     LAVVLDTALC RPVLLGGKEA NIDWELAVEK IQHVVVEQEF SPYYARRLAL KMGLQGAMMQ
     SISTVMEKMY QLFVEKDLDL VEINPLGVSS SGSVMALNGN IRVNERAIAR HPDMAAMAEK
     IANRHPGNQT NGHLRDWDGI EMHGKIGILG NGAGSVMATL DLVANAGGKP GICLNLRHAF
     PTDTPATTFS DRLTKSLKIL AADTSIQVVL INLLGTIPQP PEVAEIILAF LQHGKSELKP
     HVLRSNGNKS RRENNFPRFV IRLGGSDLNT TRDYLATIET ESDALIVVEN LDEAVAEAVH
     LAKSYRKF
//