ID A0A0P8AFW4_9RHOB Unreviewed; 679 AA.
AC A0A0P8AFW4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:KPQ17037.1};
GN ORFNames=HLUCCO18_06385 {ECO:0000313|EMBL:KPQ17037.1};
OS Rhodobacteraceae bacterium HLUCCO18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ17037.1, ECO:0000313|Proteomes:UP000050333};
RN [1] {ECO:0000313|EMBL:KPQ17037.1, ECO:0000313|Proteomes:UP000050333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ17037.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ17037.1}.
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DR EMBL; LJSY01000011; KPQ17037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8AFW4; -.
DR STRING; 1666917.HLUCCO18_06385; -.
DR PATRIC; fig|1666917.4.peg.378; -.
DR Proteomes; UP000050333; 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 GO; GO:0006099; P:tricarboxylic acid cycle; 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; 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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 481..518
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 679 AA; 68642 MW; BD44CE341C282E55 CRC64;
MQPLSRLLRP RSIAVVGGGT WCAAVVEGCR RVGYAGPVWP VHPTKTELAG VAAFPSVEAL
PEAPDAAFIG VNRQTSVDVL GALSAMGAGG AVCFASGFRE SASETGDGPA LEAALVAAAG
DMRILGPNCY GFVNLLDGAA LWPDQHGGER VERGVAIVTQ SSNLALNLTM QARGLPLAYV
VTVGNQAQTG LSEIAEGLLE DARVTALGLH VEGVGDLAAF IAMAGRARAL GKPVVVLKSG
ASDGARAAAL SHTGSLAGSD AGACALFERL GMARVKSPAE LLEALKLLHA IGPLPSGRIG
VLSSSGGEAG IISDMVADRR LQCPPLTAEQ RAGLRAALGP KVALANPLDY HTYIWGDRAA
LAQVFTAMLA PHIAIGVAII DFPRPDRCDP SAWEIVIDAC ADAAAATGVP TAILSSLTET
MPEAIAQAML ARGVVPLSGF AEGLAALEAA ARVARTDTAA VPLVPGPAEA AACLLTEAEG
KALLAGYGVP VPRGAEAASP AEAAARVAAI GFPVVVKALG LAHKTEAGAV ALNLADAGAV
EAAAERMGGT RYLVEEMVTD GVAEIIVGIL RDPAHGFVLT LGAGGVLAEM LDDTVSLLLP
ATGAEIDAAL DRLRMAPLLG GYRGRPAADR AALVAAVLAV QDCATAHADT LTELEVNPLI
ATPDRAVAVD ALIRLGEKP
//
