ID   A0A1H6CQD7_9GAMM        Unreviewed;       721 AA.
AC   A0A1H6CQD7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SEG75058.1};
GN   ORFNames=SAMN05444390_1049 {ECO:0000313|EMBL:SEG75058.1};
OS   Marinobacterium lutimaris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=568106 {ECO:0000313|EMBL:SEG75058.1, ECO:0000313|Proteomes:UP000236745};
RN   [1] {ECO:0000313|EMBL:SEG75058.1, ECO:0000313|Proteomes:UP000236745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22012 {ECO:0000313|EMBL:SEG75058.1,
RC   ECO:0000313|Proteomes:UP000236745};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNVQ01000004; SEG75058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6CQD7; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000236745; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000236745}.
FT   DOMAIN          513..550
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   721 AA;  76079 MW;  A23B87866F342256 CRC64;
     MNMQNSAGVA GQPFLGDTRR DIRPIFNPES VAIIGMSSKP GSAGQVVLNN LIDGGFKGEV
     HLVGRSGGML GDRQILTDIA ELPEGVELAI LMLPSAAVLD AVKACVARGV RGAVCFASGF
     AEMGAEGREQ QRIIAETAAA GGMTLLGPNT VGYFNYVNAF YVMMVELQLP APLDPEEGPA
     VAVVAQSGGI GAHIAASLRA RGVPLSYMMT TGNEAQTGLA DMVSYFAADE YTGAIVVYAE
     QIRSAPDFVA AVKEARSRGK GVVLLHPGRS ERSQEAAKSH TGALAGNHAA MQLMAEYAGV
     AVVDSLEEAI DVSQLLLRYP TAPVGGMGLA TASGAICGLS QDYVEPLGLE LPPLSQEQVA
     ALKEHLPDFL PPRNPLDLGT LVSFQPDLIE TGVKALLADS SIGSAMISMA MPGPEASLVW
     LKYYLAATAG SEKPAIFVMQ NEDVPLSPEF IAEARRHRAI VMRSPERAIR ALARITRFGR
     RQAMQQQQAA ALSHEALARV ELGQGVLPEW SGKQILRELS IPVPDGALAR SADEAVSIAS
     DIGYPVVIKA QSAKLAHKSE VGGVLLNIAD EAQLRNAWTQ LYANVRKAEP ELELDGALVE
     KMGARGLELV VGASRDPQWG PILMVGLGGV WVEALGDVQL LPPQLPREAI IEKLHSLKAS
     KLLSGFRGEP AVDVEAVADV VAKVGQLMVE RPEIQEIDIN PLVVYADGKG VAAQDVLVVT
     E
//