ID A0A263DLU8_9PSEU Unreviewed; 728 AA.
AC A0A263DLU8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=6-carboxyhexanoate--CoA ligase {ECO:0000313|EMBL:OZM79544.1};
GN ORFNames=CFP66_25620 {ECO:0000313|EMBL:OZM79544.1};
OS Pseudonocardia sp. MH-G8.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1854588 {ECO:0000313|EMBL:OZM79544.1, ECO:0000313|Proteomes:UP000216936};
RN [1] {ECO:0000313|EMBL:OZM79544.1, ECO:0000313|Proteomes:UP000216936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-G8 {ECO:0000313|EMBL:OZM79544.1,
RC ECO:0000313|Proteomes:UP000216936};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Non-contiguous finished genome sequence and description of Pseudonocardia
RT marinum sp. nov., an obligate marine actinomycete from a macroalgal
RT phycosphere.";
RL Submitted (JUL-2017) 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:OZM79544.1}.
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DR EMBL; NKYF01000012; OZM79544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263DLU8; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000216936; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:OZM79544.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000216936}.
FT DOMAIN 522..726
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 728 AA; 74776 MW; ED0390566C149A35 CRC64;
MDDRRGLLGD PQEPDRRVRL RPQVLPARGE QVTRTHDLAA LRGALLAPRS VALVGVSDDV
RKTGARPLQY LRRAGWAGTV YPVNPNRPLV QGERAWPSVE ALPEVPEHAY VLAGPDAAVE
VTRECARLGV QVVTIMADGF VGPDPASVAR ARALQDIVAA HAVRVVGPSS LGVVNVHERL
TLTANAAFGE PDLPEGGVFV ASHSGSVIGA LVSRGKEMGV GFAGLVSTGG EVDLSLGEIC
LSTLDDPGVE GYALFLESLA GAASLREFAA AAAERGKPVL AYKLGRSDAG AELSVSHTGA
LAGDDAVASA FLADIGIGRV DSFEALLEGQ QLVRSVPLRP RAARAPRVGV VTTTGGGGAM
AVDRLAVAGA VPQRPSEETR RALAERGIAA DHGTLVDLTL AGTRYEVMSA ALEVMVAAPE
FDVVVAVPGS SARFHPDLAV RPIADRAHTG APLAAFVVPE APEALRLLRS AGVSAFRTPE
SCADAIVAAF SRRAPRPAGS RAPAAIPGLP DAAGVLDEVA SYAVLDAVGV PHAPFTLLAP
GGDVPDVAGP SVVKAVSARL PHKSDAGAVV LDVRDADGVR RAVADIGAAL AATVPDVALE
TVMVAPMVRG LAEVLVGYRR DPDAGPIIVL AAGGVLAELY RDRSVRTAPV DLATAEEMVA
EVLALRALAG YRGAARGDLP ALARAVVGLS QLAASPRIAE AEANPVMVLA QGRGVVAVDA
LVRIEEER
//
