ID S7TR97_DESML Unreviewed; 820 AA.
AC S7TR97;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=CoA-binding domain protein {ECO:0000313|EMBL:EPR39190.1};
GN ORFNames=dsmv_2694 {ECO:0000313|EMBL:EPR39190.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR39190.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR39190.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR39190.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
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:EPR39190.1}.
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DR EMBL; ATHJ01000091; EPR39190.1; -; Genomic_DNA.
DR AlphaFoldDB; S7TR97; -.
DR STRING; 897.B2D07_17455; -.
DR PATRIC; fig|1121405.3.peg.2356; -.
DR eggNOG; COG1042; Bacteria.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000014977; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; PTHR42793; COA BINDING DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42793:SF1; PEPTIDYL-LYSINE N-ACETYLTRANSFERASE PATZ; 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:UP000014977}.
FT DOMAIN 317..414
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 820 AA; 89129 MW; 6E763BB23DB947BD CRC64;
MSLSTPPPEN TKTPPIDFEA ITRLFAAAEA AGRYFLFEYE VYDLLRASGA ETPPATRLLP
KGSRPSDADL TALPGDRVVL KIVSPAIVHK SDVGGVRIVP NTPEKVRSAW RRMMSEVPEA
YAAVMERNPT LAVADYLGLE GERLRQAVSR DIKGVLMARF MPPDSEAFGN EMIVGIRFTR
EFGMIISAGL GGTDTELYAE RFRKGQAVVA AATALTDGEA FFDLFRGTIS YRKLAGLTRG
QRRIVTDEQL VECFAAFIAM ANHYSPVNPT APYVIDTLEI NPFAFTDYLM VPLDGLCRFS
RPGTRSVPRP YWKIRRLLRP GIIALIGVSA SRVNFGRIIL NNILAAGFPA DRIRIIRPGI
TVLEGVRCVP DIGALDVKPD LLVIAVGSDQ VPDLVDLIIE RDAAHTVMLI PGGLGETRES
VQRAEQVTAA VQRAHRSPSG GPIFLGGNCL GVVSHPGRYD TLFIPDAKLS RRWEVRKRNA
AFVSQSGAFM ITRLSKRPEL DPAYMISVGN QNDLTLGDMM HYLKTDPDID VIAVYAEGFK
DLDGLDFTRA LREAVASGKD VILYKAGRTP EGKSATSGHT ASLAGDYMVC ESCIRQAGGI
PAQTFPQFED LLMLAQRLHG KRINGNRLAA LSGAGFEAVG MADNIQSDDY AMTLARFTPV
TVDRMAALLT AKGLDRLVEV GNPMDINPGA DDEAHILAVR HLAEDPNVDA VVVGLDPLSP
AMRTLATCES GRYNFDAPGS IAFELPRQVD ALDKPVVGVV DAGRLYDPLV DALVEKGMAV
FRSSDRAVRA LALYIEGRLT AERIRHGALR PGRDKPDPVI
//
