ID D1A2N2_THECD Unreviewed; 690 AA.
AC D1A2N2;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=CoA-binding domain protein {ECO:0000313|EMBL:ACY96052.1};
GN OrderedLocusNames=Tcur_0454 {ECO:0000313|EMBL:ACY96052.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY96052.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY96052.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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DR EMBL; CP001738; ACY96052.1; -; Genomic_DNA.
DR AlphaFoldDB; D1A2N2; -.
DR STRING; 471852.Tcur_0454; -.
DR KEGG; tcu:Tcur_0454; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_11; -.
DR Proteomes; UP000001918; Chromosome.
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; 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:UP000001918}.
FT DOMAIN 6..101
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 690 AA; 70592 MW; 6D8F5F3FB68B8868 CRC64;
MSLSVFSDPA SVAVVGASAD PAKWGYWIAR GALRGAHRRE VHLVNAKGAV IEGVQSARSL
SELPSAPELV VLTAPARTIP AVIDEALALG VKGFLGITAH IDAANGEAGL ERRLAERIRR
AGARIVGPNC LGLYDAGSEL ELAWGTFVPG SIAIVSQSGQ LGLELAGLAA HAGLGVSRFV
SIGNQVDVTA AELLEDLISH ETTRTVVLYL ENFGAGRELA AVMARLRQAG KHVIVLTVGA
SDAGRAAARS HTGAMTAATD VVAAACRAAG AAFVETPAQA IDLAHLLIDG PLPAGDRVAI
VSDSGGQGAI AADTLSRHRL TVPALSEGTR AAVAALLPEG AGTANPIDLA GAGEQDLATY
ARLVDVLLGS GEVDTVVLSG YFGCYGADTP SLVDRELQVA DAIAASAARH GRPVIVHSMS
HDSQAVRRLR SRAVPTLFTI DAVARSLGIA AELARSAPAD PARLAAPAAP LGDTGKALPY
LAGRDLLAKA GLSYPRAIAV WTPEEAGTVA RSMTGPFVLK AGWLEHKTEL GGVAVGLPDA
DAVRAALADM ISRLGEGDYV LEEMDTRTGA VELIVGARRD PAFGPVVLVG LGGVTAELYR
DVALALAPVD VAEARRLLES LAGLPLLTGF RGRPAVDVDA VAESVVAVSR LIAEDGRVLE
CEVNPLRVGP DGAIAVDALV VAAAGDQPDW
//
