ID   A0A1H3HMY2_9PSEU        Unreviewed;       736 AA.
AC   A0A1H3HMY2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SDY16863.1};
GN   ORFNames=SAMN05216215_102118 {ECO:0000313|EMBL:SDY16863.1};
OS   Saccharopolyspora shandongensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=418495 {ECO:0000313|EMBL:SDY16863.1, ECO:0000313|Proteomes:UP000199529};
RN   [1] {ECO:0000313|EMBL:SDY16863.1, ECO:0000313|Proteomes:UP000199529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3530 {ECO:0000313|EMBL:SDY16863.1,
RC   ECO:0000313|Proteomes:UP000199529};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNOK01000021; SDY16863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3HMY2; -.
DR   STRING; 418495.SAMN05216215_102118; -.
DR   OrthoDB; 190266at2; -.
DR   Proteomes; UP000199529; 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; 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;
FT   DOMAIN          262..356
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   736 AA;  76909 MW;  86831A31E83F3510 CRC64;
     MSVDTSRPSI QDGIAALVSE ARSRESAMFT EAQAKSLLAI FGIDVPRGVQ VSDGELIPEH
     LGESLVVKAI SSTLVHKSDA GGVRVGVSRE QVAEVTDQMR KRLAASGHRL SGLLVEEMVP
     AGHEVIVGAT KTPDLGWSVM VGLGGVLVEV LEDVAFGLAP LSEDQTLRML RELRGIKVLE
     GARGGVRADL SPLVRLISRL AGPGGLLESL PEDVVELDLN PVIVSADRAV AVDARFVVSA
     EEAADAEAEA RPERPAPDFS ALFRPARVAV LGASGKRPNL ANRYIRNLRA GGFEGTIVPI
     HPEADDIEGL PAVTSLADTD EPIDYAFVAL PAARVSEALL AAAGRVRFAQ VIASGFGETE
     EGKPLEKTLV ETVRRAGIRL IGPNCLGTHA SAGRLSFIPD APLTPGVTAV VSQSGGLSVD
     ILRVGAMRGI DFHSVVSIGN GADVNAAELV ASHLADDDVR VIGLYLESLA AAREVLDVLT
     TGEVRKPVVL LAGGRTSEGS RAATSHTGAL AGNHRLWQAI ARQAGMTLVD SLEDFASALH
     ALSTIDLDIR STGRQAILFG NGGGASVLGA DALDRQGLST SPLADSVIRQ LDGLGLPPGN
     GLRNPIDVPA GTLAVRNGQV AEDMLKLVLA GSEPDILISH LNVGIIQRNL GESHGDVTGT
     IIDSIVHVRD EANSNTHHLL VLKTDGSQKT EELITGYAHR ARSSGIPVFA AFEDAALAAR
     AVLEQTHQGC EDDGRR
//