ID S4MZ55_9ACTN Unreviewed; 714 AA.
AC S4MZ55;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=STAFG_1552 {ECO:0000313|EMBL:EPJ41400.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ41400.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ41400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ41400.1};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) 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:EPJ41400.1}.
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DR EMBL; AOPY01001321; EPJ41400.1; -; Genomic_DNA.
DR RefSeq; WP_020270549.1; NZ_KE354065.1.
DR AlphaFoldDB; S4MZ55; -.
DR PATRIC; fig|1283301.3.peg.1532; -.
DR HOGENOM; CLU_007415_2_2_11; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000015001; 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:UP000015001}.
FT DOMAIN 30..66
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 714 AA; 75323 MW; 27D6E35494383CAA CRC64;
MAEDRVLRVR GVLDSVRAEG RTALTAPEGK VIADAYGIAV PGEELATDVD EAVAFAARFG
GPVVMKIVSP DILHKTDAGG VIVGVEGAAD VRAAFHTIID NARAYDPKAR ISGVQVQELL
PQGQEVIVGA VTDPTFGKVV AFGLGGVLVE VLKDVTFRLA PVDADEALSM LDSIRSAEIL
RGVRGQAGVD RWAVAEQIRR VSELVADFPE IAEVDLNPVI ATAEGAVAAD IRIILAESQP
APRRKYSRDE ILTSMRRLMQ PGSVAVIGAS NEQGKIGNSV MRNLVDGGFA GDIHPVNPKA
DDILGRKAYK SVTDVPGEVD VAVFAIPAKF VAAALEEVGR KGIPNAVLIP SGFAETGEHE
LQAEIVAIAE RYGVRLLGPN IYGYYSTWHD LCATFCTPYD VKGGVALTSQ SGGIGMAILG
FARTTKTGVS AIVGLGNKSD LDEDDLLTWF GEDPHTECIA MHLEDLKDGR AFVEAARATV
PKKPVVVLKA GRTAAGAKAA GSHTGALAGD DAVYDDILRQ AGVIRAPGLN DMLEYARALP
VLPAPKGDNV VIITGAGGSG VLLSDAVTDN GLSLMEIPPD LDEAFRKFIP PFGAAGNPVD
ITGGEPPSTY EATIRLGLED PRIHALVLGY WHTIVTPPMV FAELTARVVA EFRERGIEKP
VVASLAGDVE VEEACQYLFE RGVVAYPYTT EKPVAVLGAK YRWAREAGRL GGGT
//
