ID A0A3S3ZPQ8_9MICO Unreviewed; 684 AA.
AC A0A3S3ZPQ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:RWZ50825.1};
GN ORFNames=ELQ90_08265 {ECO:0000313|EMBL:RWZ50825.1};
OS Labedella phragmitis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=2498849 {ECO:0000313|EMBL:RWZ50825.1, ECO:0000313|Proteomes:UP000288547};
RN [1] {ECO:0000313|EMBL:RWZ50825.1, ECO:0000313|Proteomes:UP000288547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11W25H-1 {ECO:0000313|EMBL:RWZ50825.1,
RC ECO:0000313|Proteomes:UP000288547};
RA Li F.;
RL Submitted (DEC-2018) 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:RWZ50825.1}.
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DR EMBL; RZNB01000003; RWZ50825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3ZPQ8; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000288547; 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}.
FT DOMAIN 480..683
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 684 AA; 69482 MW; EE801F3C0F885144 CRC64;
MPPRDLVPLL APRGVVVVGA SGNPEKLGYA MASSLKTFPG DVRLVNSRPT AGMHSSIAEA
AAAGGVPDLA IMCVPATHTA SAVRESAEAG IGAALVCAGG FAEAGGVGVD YARDLDTVVA
ETGIRLLGPN TSGFFVPDAA LFASFVPGVR RLGAGSVAVV AASGGINHVL SFRLESDGAG
VSLGVGIGAG QDVSAPDVLQ YLIDHEPTRA VILHVETVPD GRALMTAVAE LAVVKPVVAL
VVGRNDVSEF ARSHTGALAT SWRTTRAALR QAGAVLVGDE AQAVAAATAL SARRARASAR
PGVALITAQA GPGLLIADAL GDANHLPALG RDTQGALADL LPPLTFQANP VDTGRPSETF
PAVVRTVAAD PVTDVLGVYA ITEPVVDIVT DVLAADISDG IPVVIGVDGP ASEVSDIRRS
GRESGVPVLS GPNQLAHGLA ALTDDARARA VRPEAAISSP VVPPWVASVA DEGWDEARGK
DLLDALGVPT PPRYRCADRD EARRAWRELD APLAVKLLDA SVLHKTEVGG VVLGVRTTDD
LERALDVLEA AGASEFLVES MAGPGVDLVV GARNDDVFGP IVAVGVGGIA TEVLGDVAIR
TAPLAHTVAV AMTEDLVARE LLLGHRGGAA VDLDVLADIV VRLGALVADG VVDEIEINPL
RSTPSGIVAL DAIVLPAHKE VRTS
//
