ID A0A0S8CB62_9BACT Unreviewed; 714 AA.
AC A0A0S8CB62;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 16.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:KPK20990.1};
GN ORFNames=AMK69_22785 {ECO:0000313|EMBL:KPK20990.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK20990.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK20990.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK20990.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK20990.1}.
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DR EMBL; LJNR01000523; KPK20990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CB62; -.
DR PATRIC; fig|1704023.3.peg.3703; -.
DR Proteomes; UP000051394; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR043938; Ligase_CoA_dom.
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; PF19045; Ligase_CoA_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}.
FT DOMAIN 504..540
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 714 AA; 77882 MW; ECC0287249B459DC CRC64;
MSLEKILDAE SVAIVGASKT ETKRGFQAIR TLLDEKFQGN IYPVNPKEKS ILGFKCYENV
SDIEDSVDVA LITTPAKTIP AILEDCGKKG VKGAVVIAGG FGEIGKEGRK LEDEMVAVAR
KHNIRLIGPN TSGMMNLKDN LNLVGLRDAP RGDIALLSQS GNMALTLITE AKIKSRKGFS
YYVGVGNEAD IKFHEYLDFF RKDPDTKAIL IYVEGMRQGR EFLQQAYKTT IEKPVILLKS
GRTATGKRSA GSHTGALAGI SEVAKGAFER AGIIVIENSD ELFPVAETLS SLPPIKNNSV
AILADGGGHA TIAADLLTDL GLMISELSGK TQAKLKKILP FAASVPNPVD VAGGADADPA
IFAECAEIIL KDPSVGGLLV VGLFGGYGIR FAESLALAEE GAAHMMGKLV KKRKKPIVLH
SLYSPEKPHA LDLLRYYNIP VYDSLDVACK CIGVLAEYGR FLEQYHARAK FVFNWREKAT
SKGSEIIRQV KEDGRAFLLE YEAKQLLHSH GVPVPKDHLA KTVDEAVSIA RDIDGEVVLK
IVSPDILHKS DAGGVRLKLR TEREIRNAFD EIVENAKRFD PNADIRGVLV SPMAKEGMEV
IIGTKIDDQF GPIIMFGMGG VLVEILRDVS FRVLPISPYS ARKMIKEIRS APLLDGYRGV
VPRDKKVLKR LLLRCSDIIE AYPAIQEMDL NPVIVYERGL SVVDARIIIK DKVS
//
