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Database: UniProt
Entry: A0A0F4QWB7_9GAMM
LinkDB: A0A0F4QWB7_9GAMM
Original site: A0A0F4QWB7_9GAMM 
ID   A0A0F4QWB7_9GAMM        Unreviewed;       705 AA.
AC   A0A0F4QWB7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:KJZ12001.1};
GN   ORFNames=TW85_16475 {ECO:0000313|EMBL:KJZ12001.1};
OS   Marinomonas sp. S3726.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ12001.1, ECO:0000313|Proteomes:UP000033747};
RN   [1] {ECO:0000313|EMBL:KJZ12001.1, ECO:0000313|Proteomes:UP000033747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3726 {ECO:0000313|EMBL:KJZ12001.1,
RC   ECO:0000313|Proteomes:UP000033747};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(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:KJZ12001.1}.
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DR   EMBL; JXYC01000020; KJZ12001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4QWB7; -.
DR   PATRIC; fig|579484.3.peg.3373; -.
DR   Proteomes; UP000033747; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033747}.
FT   DOMAIN          1..96
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   705 AA;  74697 MW;  20513204438D99BD CRC64;
     MLAPDSIAIV GASNDPTKRG YKAMMGLIDG GYQGDIYPVN PKADTILGKP AYASVNLIPE
     GVHMALICTP ASTIPSLIKE CGDVGVKGAI ILASGFGEVN EAGAKLEQAV LEAAKKAGVR
     VIGPNTSGLF NLHKKVNLLA LDNVRAGDIG IISQSGNMLL SLALEAQSNG HIGFSTYVGP
     GNQTDVGFAD YLAYLGSDKH TGVATFYVEG FKGGRAFLDE AKRTSQLKPV VVYKSGSTEA
     GQKAASSHTG ALAGSYQMTV DLLQQAGVSV VANSDEILPV AEGLGLMRHA SGKRVAVLAD
     GGGQATIASD RISEAGLELA ELEPATRLAL SQILFPQASL VNPIDVAGST DAAPGLLSKC
     MEILVADKNV DMVFLVGMFG GYGIRFAKEL IEEELQCADE MIALAKKTDK PLIIDSLYAH
     IKPEPLEKLR QAGLPVYASI EHAVKIMSAL GERGAYLKNN QRQARKAPLT INQACADSLA
     NAKNQGRDLF EYEAKNLLSA YGLEVAKEII VRNESELEGV FAEFGDIPLV MKVVSKDILH
     KSDAGGVKLN LVGKNALYTA RESILASCLA YNDDADIEGV LITPMARKGT EVIIGMSQDP
     IFGPVLMFGL GGIFVEILKD VSFRAIPLSR YDAISMIDQI KASKVFDGVR GELPLDKDAL
     VDLLLTVSAI VENHPDISEL DLNPVIAYDK AYAIVDARII VSQEK
//
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