ID A0A2S6NMK8_RHOGL Unreviewed; 702 AA.
AC A0A2S6NMK8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=CCS01_03875 {ECO:0000313|EMBL:PPQ37117.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ37117.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ37117.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ37117.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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:PPQ37117.1}.
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DR EMBL; NHRY01000051; PPQ37117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NMK8; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000239724};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 13..107
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 702 AA; 73600 MW; 090927CAB5FE45EB CRC64;
MSQPAGPRDL STMLQPRSIA LIGATDRSGW SRMTYANLSN GTYKGEVHLV ARRGGTVHGR
TAATSCAALG TKVDLGLIMV PAAAIEEAVA DLGASGARNA VILTSGFAET GLDGVAQQRK
LAELARRFNI SILGPNCLGF VNFLDGVPLW TGSFRSPSQP GPIAAISQSG ATGAFIASLA
EQQQIGLSHL ISTGNEADLD GATFAAHLLE DDRVRAIAMF IESIRDPHRF AAAAQKAQAA
GKPIVALKIG LSDVTARSAQ AHTGALVGDD RVFDGACRQF GVVRVQSIED LLFTADIIAR
TGVIGAKGVG LVSVSGGACE IAADRLQAEG VPLPPLPPAT EKALIDVLPS FGTPHNPLDI
TGGAVLEPNL FERALKIVGG EPAFSALVCL FDVPGVDAQA SEFQLAALRH ISQGLAKQPL
PALMLSHTMK PVTEVTQRIV ADLDLPYSSA GMFHGLSALG RAWWWSEQQR RERHAWMPPA
QSQGLAVWPT TERQVLDHLA RYDVPIVPAT LVTDEATAVA VARDAGGPVA LKIASADIQH
KSDIGGVALN VSGDSHVAAA FRRVMAAAPA RARVDGVLVS PMRERGLELF VGCTRDPQWG
PVLAVGLGGI FVEVLQDVAL RVLPVTPAEV RRMLRELKGA RMLQGQRGVP PADLDAVAET
IARIGDAALA LGTKLDELDV NPLWVRGAQV EALDALAVAR AT
//
