ID A0A0Q8RGZ5_9BURK Unreviewed; 695 AA.
AC A0A0Q8RGZ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=6-carboxyhexanoate--CoA ligase {ECO:0000313|EMBL:KRB93513.1};
GN ORFNames=ASE07_12475 {ECO:0000313|EMBL:KRB93513.1};
OS Noviherbaspirillum sp. Root189.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB93513.1, ECO:0000313|Proteomes:UP000051303};
RN [1] {ECO:0000313|EMBL:KRB93513.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB93513.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB93513.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB93513.1,
RC ECO:0000313|Proteomes:UP000051303};
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:KRB93513.1}.
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DR EMBL; LMHZ01000003; KRB93513.1; -; Genomic_DNA.
DR RefSeq; WP_057289250.1; NZ_LMHZ01000003.1.
DR AlphaFoldDB; A0A0Q8RGZ5; -.
DR STRING; 1736487.ASE07_12475; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000051303; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:KRB93513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051303}.
FT DOMAIN 15..110
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 695 AA; 72082 MW; 4C02F665C2858C63 CRC64;
MNATSTSGAA LAQALLNPRS VALIGASDDT GKTAGRPLQY LRRTGFKGAV YPINPKRATV
QGEQAWPDLA SLPEVPDHVF VLTPTEGVLP AVEECARVGV KVVTVLAAGF SESGPEGAAR
EQELSAISKR TGIRVLGPSS LGVVNPSTGL VLTANAAFAE PDLPVGRVFV ASHSGSMIGA
LVSRGKARGV GFAGLVSVGG EADLSIGEIC AATLDDPSIE GYLLFLETLH HGPKLRDFAI
EAARRGKPVI AYKLGRSDAA AEMAATHTGA LAGEDDVADA FLKDCGIARV GILEALLESF
PLAKRVKLTA SASMPRRVGV VTTTGGGAAM AVDQLGIRDV VVQPASEQTM QRLAAAGVSA
NPGRVLDLTL AGTRYEVMKK TLDIMLDAPE FDLVLAVVGS SARFQPQLAV KPIVDSVQGA
KPLAAMLVPD APDALAALTA AGVPCFRSPE ACADTIASVF ARRLPGVAPR VVERSSVDTH
TLSEEQAYAV LDELGVPHAP VVTMSLSTPA PALPFDFPVV AKICSEHISH KTEVGGVVLG
INSDVELNQA LATLRNNLAE RAPGIACDQA LVQPMLKGLT EVLVGYRIDP DAGPIIMLAA
GGIWAEVSRD RSIRLAPVSV DTAREMIAEV RSLKTVSGLR GKRRGDLEAL AHTVSALSQL
AMKPELGVCE AEVNPLMVMP EGEGVLAVDA LVLKA
//
