ID A0A117RS31_9ACTN Unreviewed; 714 AA.
AC A0A117RS31;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:KUO06169.1};
GN ORFNames=AQJ67_03305 {ECO:0000313|EMBL:KUO06169.1};
OS Streptomyces caeruleatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=661399 {ECO:0000313|EMBL:KUO06169.1, ECO:0000313|Proteomes:UP000053429};
RN [1] {ECO:0000313|EMBL:KUO06169.1, ECO:0000313|Proteomes:UP000053429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUO06169.1,
RC ECO:0000313|Proteomes:UP000053429};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT strain for the species Streptomyces caeruleatus.";
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:KUO06169.1}.
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DR EMBL; LMWY01000003; KUO06169.1; -; Genomic_DNA.
DR RefSeq; WP_062716782.1; NZ_KQ948924.1.
DR AlphaFoldDB; A0A117RS31; -.
DR STRING; 661399.AQJ67_03305; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000053429; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR043938; Ligase_CoA_dom.
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; PF19045; Ligase_CoA_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:UP000053429}.
FT DOMAIN 30..240
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 714 AA; 75536 MW; FB5BE0C630279F3D CRC64;
MAEDRVLRVR TLLDSVRAEG RTALTAPEGK VIADAYGIAV PGEELATDVD EAVAYAARFG
GPVVMKIVSP DILHKTDAGG VIVGVEGAAD VRAAFHKIID NARAYNADAR IEGVQVQELL
PQGQEVIVGA VTDPTFGKVV AFGLGGVLVE VLKDVTFRLA PVDADEALSM LDSIRSAEIL
RGVRGQAGVD RWAVAEQIRR VSQLVTDFPE IAEVDLNPVI ATAEGAVAAD IRVILSEAPA
KQRRRYSREE ILTSMRRLMQ PASVAVIGAS NEQGKIGNSV MRNLIDGGFA GDIHPVNPKA
DDILGRKAYK SVTDVPGEVD VAVFAIPAKF VAAALEEVGR KKIPNAVLIP SGFAETGEHE
LQAEIVEIAE RHGVRLLGPN IYGYYSTWQD LCATFCTPYD VKGGVALTSQ SGGIGMAILG
FARTTKTGVS AIVGLGNKSD LDEDDLLTWF GEDPHTECIA MHLEDLKDGR AFVEAARATV
PKKPVVVLKA GRTAAGAKAA GSHTGALAGD NAVYDDILKQ AGVIRAPGLN EMLEYARALP
VLPAPEGDNI VIITGAGGSG VLLSDAVTDN GLSLMEIPPD LDEAFRKFIP PFGAAGNPVD
ITGGEPPSTY EATIRLGLED PRIHALVLGY WHTIVTPPMV FAELTARVVA EFRQRGIEKP
VVASLAGDVE VEEACQYLYE RGVVAYPYTT EKPVAVLGAK YRWARAAGLL GGGS
//
