ID A0A418Y5N0_9BURK Unreviewed; 706 AA.
AC A0A418Y5N0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:RJG22071.1};
GN ORFNames=D3872_05860 {ECO:0000313|EMBL:RJG22071.1};
OS Massilia cavernae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=2320864 {ECO:0000313|EMBL:RJG22071.1, ECO:0000313|Proteomes:UP000284006};
RN [1] {ECO:0000313|EMBL:RJG22071.1, ECO:0000313|Proteomes:UP000284006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-61 {ECO:0000313|EMBL:RJG22071.1,
RC ECO:0000313|Proteomes:UP000284006};
RA Zhu H.;
RL Submitted (SEP-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:RJG22071.1}.
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DR EMBL; QYUP01000063; RJG22071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418Y5N0; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000284006; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000284006}.
FT DOMAIN 497..704
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 706 AA; 73438 MW; 4159B41468B07A15 CRC64;
MNNHQAPITQ ASLGRLLRPR SIALIGVSAE PGSAGGAVLS NLERFGYQGN IHLVSRTQKE
VHGRPCVASV DDLPHGVDVA VLGVPQAAIL GTLESCAARG VGAALVFASG FAETDAAGKA
AQLELATVAG RNNLPVLGPN CLGFVNYIDN VPLTFEAVPP TKGAAGVAVL AQSGAMAANI
RMALVSRGCP VAYAISTGNE AVVAVEDLLE WLIDDPHTHA ISLLVEQIRN PERFLALAEK
AMSHGKPLVM LHPGRSERAR DAAMSHTGAM AGNYSIMAVL AAASGVVHVD TLDELFDVTL
LLNRFPSGAA GGTAILTNSG ACKGVALDFA EAIGLELPLL APETVSSLQA LLPAFASAEN
PLDITTAGMK DASLFGTTAM TLLDDPGVGS LVVTVMGGSP GQQLAKANAL VPCLSKSTKP
AVIAYMGDDS PLAEGLSDVM RAGAVPFFRS PERAMRAMRA LANYWRVAQT MGSREAGPQV
PAAEFPRRGL LAEYQAKALL APLGLAMPRG GLAKTVNEAI DIAREIGYPV VMKAQAPELP
HKSDVGGVAI KIADAAGVRD AWERIRTSVL RARPELELDG LLVESMAPSG LEMVVGARRD
PEWGAVVLIG LGGIWIETLK DFRLIPVAAS RQQVLAEIEK LRGAALLHGT RGAPALDIEA
LADSIMLLAA VMRANPELVE IDINPLVVFE AGKGVLALDA LMVTRS
//
