ID A0A0Q5Z5Y2_9BURK Unreviewed; 697 AA.
AC A0A0Q5Z5Y2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:KQT13325.1};
GN ORFNames=ASG30_20430 {ECO:0000313|EMBL:KQT13325.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT13325.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT13325.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13325.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT13325.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13325.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQT13325.1}.
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DR EMBL; LMQL01000004; KQT13325.1; -; Genomic_DNA.
DR RefSeq; WP_055893300.1; NZ_LMQL01000004.1.
DR AlphaFoldDB; A0A0Q5Z5Y2; -.
DR STRING; 1736365.ASG30_20430; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP 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; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051173}.
FT DOMAIN 8..103
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 697 AA; 73243 MW; 546C3BDAF1703F5A CRC64;
MAHRLDPLLA PRSIAVLGAS NDPARIGGMG IDLLRHFGYP GTVYPVNPKY KLVQGLESYP
DVASLPEAPD LVVVAIAAPE VTAALRQCHA RGIRAAIVYG AGFAEAGAAG AALQRDLEAF
AAESGMVIAG PNCMGFANLN ARVFTAFAGV FRATAPQERP GRVSLLTQSG NVCAAVFALL
RGVDVGVSHF INTGNEATLE FSQYLDYLVQ DDATDCVVGY VEQLRDGPAF IDAAVRFARA
NKPLILYKAG ETEKGAEAVR SHTSALAGNL ALYRTAFRQL NVIQAEDFAQ MADLAMLSAL
RDRTAGRRVG VLTLSGALGA ILADKFSAAG LEVPTLPAAT QARFRGVIPD YGMVSNPVDC
TGNIVNDPGR AASILEALAT APEVDVVVIY AMGALLDRMA DPLMDVVRRH GRLFVVIDTG
LAKRRAELAA AGVPVFTDLG RAVQAIAPFC RWHAGRAATL RWAGLRDAAG TDRETLHEAP
NEYESKRLLA RYGVEAVAEA PAGDEATAVA QAQRLGFPVA LKILSADIAH KTEIGGVRLN
LGDADAVRMA CRQVLAAARE RAPGARIDGV LVQKMSTGVA ELIAGVTRDE VFGAALTVGL
GGVLTEIYQD VSHRLLPVDE TLAREMLGEL KARALLEGFR GRPRGDVAAA AAGIAGLARA
AEALRGSVRE IEVNPLLVRA EGEGAVALDA LLLPEAR
//
