ID B4S9V9_PELPB Unreviewed; 398 AA.
AC B4S9V9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=ATP-grasp domain protein {ECO:0000313|EMBL:ACF43655.1};
GN OrderedLocusNames=Ppha_1392 {ECO:0000313|EMBL:ACF43655.1};
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF43655.1, ECO:0000313|Proteomes:UP000002724};
RN [1] {ECO:0000313|EMBL:ACF43655.1, ECO:0000313|Proteomes:UP000002724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC CoA ligase alpha subunit family. {ECO:0000256|ARBA:ARBA00005899}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC CoA ligase beta subunit family. {ECO:0000256|ARBA:ARBA00010719}.
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DR EMBL; CP001110; ACF43655.1; -; Genomic_DNA.
DR RefSeq; WP_012508146.1; NC_011060.1.
DR AlphaFoldDB; B4S9V9; -.
DR STRING; 324925.Ppha_1392; -.
DR KEGG; pph:Ppha_1392; -.
DR eggNOG; COG0045; Bacteria.
DR HOGENOM; CLU_006587_3_1_10; -.
DR OrthoDB; 9802602at2; -.
DR Proteomes; UP000002724; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.30.470.110; -; 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; IPR032263; Citrate-bd.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002724};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..242
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 398 AA; 43765 MW; B1AF45A326632AB5 CRC64;
MAKILEGPAM KLFNKWGIPV PNYVVIMDPD RLAQLGEANK WLRESKLVVK AHEAIGGRFK
LGLVKLGLNL DEAYAAAKEM IGRQIGTSVV RQVIVAEMLD HDEEYYLSIA GNRDGSELLL
SNKGGVDIED NWDTVKRLVI SLDETPTIEH ITEAALEAGF TGEVAERVAK IASRLILCFD
NEDAQSIEIN PLVIRKSDMR FAALDAVMNV DWDARFRHAD WDFKPVSEIG RSYTEAEQQI
MDIDARIKGS VKLVEVPGGN IALLTAGGGA SVFYSDAVVA RGGSIANYAE YSGDPPDWAV
EALTETICRL PNIKHIIVGG AIANFTDVKA TFNGIINGFR ESKSKGYLEN VQIWVRRGGP
NENQGLAAMK KLQEEGFDIH VYDRSMPMTD IVDLALNS
//
