ID A0A102D903_9SPHN Unreviewed; 706 AA.
AC A0A102D903;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:KUR77166.1};
GN ORFNames=AQZ49_10230 {ECO:0000313|EMBL:KUR77166.1};
OS Novosphingobium sp. FSW06-99.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR77166.1, ECO:0000313|Proteomes:UP000061032};
RN [1] {ECO:0000313|EMBL:KUR77166.1, ECO:0000313|Proteomes:UP000061032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR77166.1,
RC ECO:0000313|Proteomes:UP000061032};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) 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:KUR77166.1}.
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DR EMBL; LLZQ01000013; KUR77166.1; -; Genomic_DNA.
DR RefSeq; WP_067615181.1; NZ_KQ954255.1.
DR AlphaFoldDB; A0A102D903; -.
DR STRING; 1739113.AQZ49_10230; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000061032; 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 Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 498..549
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 706 AA; 72552 MW; EDC72C4EB14AB796 CRC64;
MSDTSPRFAR AALARLLRPK SVAVVGASDK PGALGATLIT NLDRAGFAGD VWPINPKRDT
IGSRKCLPGI ADLPMGVDVA VLAIPRPAVL DAVRALAARG VGAAIVFSAG FAEDGPEGLA
EQAEIAAVAD AAGMVIEGPN CLGLVNHVDK IPLTFVEAFC EPPAGRRAVG VVSQSGAMAA
VVGTVLIARA IPTSFSVSTG NEAVSGVEDY VDWLIDDPDT QVIAMIVESF RKPARFLAAA
RRARAAGKPI VLLHPGTSSA ARESAATHTG AMAGDYQLMR AKVARAGVIF AETLQELGDL
AELLVRCPAL ARPDIAVLGE SGAFKAMVLD QAERLGLPLT ALDNANAPAL RAALPPFVPV
SNPLDLTAQG LSQPSLYTQV ITALLDDDRV GAVVAGIIQS DPATADIKVP AILAALDGRA
LTKPMIFAGL DEGARMPDHY IAALRARGVP WFPTTERVLA ALARLGLARG PADGAAIAPL
PLPALADEAG VVPEYRAKAL LAPLGVPFPA GAFAADADAA VAAAQGLGYP VAMKAQASAL
SHKSDAGGVI LNLADDDAVR AAWYRMHASV AAYDATIALD GVLIEAMGPR GVEMIVGGRN
DPEWGAVVLA GFGGVTAEIL QDVRLFTPDM TEAEVIADLG KLKSAALLAG WRGAPALDVP
ALARLIVTVA RLLESEPRLA ELDLNPVILY PAGEGVIALD ALIFAQ
//