ID A0A196NER4_9SPHN Unreviewed; 715 AA.
AC A0A196NER4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=A7X12_14000 {ECO:0000313|EMBL:OAN65858.1};
OS Sphingomonas sp. TDK1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=453247 {ECO:0000313|EMBL:OAN65858.1, ECO:0000313|Proteomes:UP000078445};
RN [1] {ECO:0000313|EMBL:OAN65858.1, ECO:0000313|Proteomes:UP000078445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDK1 {ECO:0000313|EMBL:OAN65858.1,
RC ECO:0000313|Proteomes:UP000078445};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-2016) 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:OAN65858.1}.
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DR EMBL; LXVY01000005; OAN65858.1; -; Genomic_DNA.
DR RefSeq; WP_064310749.1; NZ_LXVY01000005.1.
DR AlphaFoldDB; A0A196NER4; -.
DR STRING; 453247.A7X12_14000; -.
DR Proteomes; UP000078445; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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.
PE 4: Predicted;
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 10..105
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 693..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 74285 MW; D788C6C6256933E7 CRC64;
MATRQSLTPL LHPRSVAVIG ASGDVTRIGG RALRHLVQVG FEGGIFPVNP TRIEVQGLKA
WARIEDIPTT PDCAIIALPT GAVLPAIQAC ARKGVRAAVI FSSGFAELGA EGERLQQQIV
ADARAHGMRL LGPNCLGAYN LHARSFLSFS GICDDVAGTA GRLGLVSQSG GYAGEVVKSA
GDVGLAFGVW ITTGNEADIG LGEALGYLAT SKDVDVVVGY IEGVRDPAAF YEALAAAHAR
RKPVIVLKVG RTDQGARAAA SHTASLVGSD AVYDAVFARF GVYRARTTEE MLDVAYAASR
GRFPHGKRLA ILTNSGGIGV QAADFAADEQ LEVAAVSPEV QRELVAISPN GAPFNPIDLT
GQVANDPPMF ARAIDAVLGS GEFDMAYCNV GLIAGLPFIE KPLLHGLTEA AQRFADLPMA
VSVTAPDAIV NAYQEAGYLC YREPARAIKA LAALAQFHAA WATPLPPRSA QGRSPRIEAG
ARFSEADGKA LLAAIGIASP TEYLVADAAG AHDAARRING PVAIKVVSAD ILHKSDVGGV
ALNVAPGSAA DCVAAMQATV SAKSTGRIGG YLVSPMITEG VECFVGTHND PLFGPTVTFG
LGGVAVELLK DVTTRLAPVS AAEATEMIRG TRSFPLLDGF RGRRRADIPA LARAISAVSH
LAAVNADSVR TIEINPLRVL DEGKGAIALD AVIETRPRHP TQPPQDISSQ GEQRA
//
