ID   A0A1I5GLL6_9RHOB        Unreviewed;       679 AA.
AC   A0A1I5GLL6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SFO36885.1};
GN   ORFNames=SAMN04487859_1334 {ECO:0000313|EMBL:SFO36885.1};
OS   Roseovarius lutimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1005928 {ECO:0000313|EMBL:SFO36885.1, ECO:0000313|Proteomes:UP000198599};
RN   [1] {ECO:0000313|EMBL:SFO36885.1, ECO:0000313|Proteomes:UP000198599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28463 {ECO:0000313|EMBL:SFO36885.1,
RC   ECO:0000313|Proteomes:UP000198599};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOVP01000033; SFO36885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5GLL6; -.
DR   STRING; 1005928.SAMN04487859_1334; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000198599; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          481..674
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   679 AA;  69695 MW;  C9EAAE4C0D3CA87F CRC64;
     MRDLSRLLRP ASIAVVGGGA WCASVVEQCS KIGYDGPVWP VHPARDEIAG RAAFASLDDL
     PGVPDAVFIG VNRETTLDVV ARLSAMGAGG AVCFASGFRE MQAETGDGDA LQARLLEAAG
     AMPILGPNCY GFINYLDGAL LWPDQHGGQR VDSGVAILTQ SSNIAINLSM QTRGLPIAYL
     MTAGNQAQLG LAQLGRALLA DSRVTALGLH IEGIGDLAAF ETLAQEARAL GKPIVALKAG
     KSEQARAAAI SHTASLAGSD AGARALLARL GVAQVEGLPA LLETLKLLHL AGPLPSNRIV
     SLSCSGGEAS LMADSAVGRD LVFPALDASQ IDGLRAALGP RVALANPLDY HTFIWGDVAR
     MTDTFAAMLM GDVAMGCVIV DFPRPDRCDP SAWDCVIEAG AAARARANKP LAILSTLPET
     LPEAVIAGCL AAGLIPLVGL GEGLTAIALA ARLGRRHDMP EPILPPGAPI NLHMLSEAEA
     KHALAGFGLS VPASRLAATP QQAAHAAGMV GFPVVLKGQG LAHKSEAGLV ALNLTDAAAV
     ANAAAAMDSS GFLIEAMVTG GVVELLVGVL RDPAHGFVLT LAAGGILTEV MADSQSLLLP
     VQETDISDAL KRLRIAPLLA GYRGKPGVDI AAIAQAVMAV QAYVIANAMR LDEIEINPLI
     CGKNFAIAAD ALIRIGEDE
//