ID F3YUW8_DESAF Unreviewed; 697 AA.
AC F3YUW8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=CoA-binding domain protein {ECO:0000313|EMBL:EGJ49145.1};
GN ORFNames=Desaf_0794 {ECO:0000313|EMBL:EGJ49145.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49145.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ49145.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49145.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
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DR EMBL; CP003221; EGJ49145.1; -; Genomic_DNA.
DR RefSeq; WP_014258978.1; NC_016629.1.
DR AlphaFoldDB; F3YUW8; -.
DR STRING; 690850.Desaf_0794; -.
DR KEGG; daf:Desaf_0794; -.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_7; -.
DR Proteomes; UP000007844; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844}.
FT DOMAIN 489..525
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 697 AA; 74161 MW; 31A979AF357D2FBC CRC64;
MDLQALFSPQ SVAVIGASAT PGKIGHTVLK NMIDAGFPGR LIPVNPKGGE IEGLPAVTSV
AELPRGLDLG VICIPRQFVL DSLRELAAIG ARAAIVITAG FKEVGRSGYH LEQEMAGIAR
EHGMALLGPN CLGLIDTAAR VNATFATGKP QPGSIAFFSQ SGALCVAILD WAAGAGVGFS
SFVSLGNKAV LDEADMLQWL GRDDKTRVIL GYLENVQDGQ TFLARATEVT RNKPVIMLKS
GTTAAGARAA SSHTGAIAGS DQAYGAAFHK AGIIRAERVS ELFDLARAFA TQPLPKGPNL
AVVTNAGGPG ILAADAAERS RLIMASLSPS TLDKLKAFLP AYASLYNPID IIGDADAERF
RKTLAAVAAD EHVHSLLVVL APTATADVEA IAKAVTRIAR ESGKPVFGCF MGSQGVVAGH
SILMEAGVPV YQFPEPAIAS IEALARYAEW RASPEPEWVE ITRDLNEARR IIEEARRWGV
REIVEFQAQE LLRAYNLPTP QTRLARSSEE AATAAGEIGY PVVLKIASAQ ISHKSDVGGV
AVGLKNLKEV LHAFTDITSR AQRMRPEAYI MGCLVQAMAP KGSREVIVGF KRDDQFGPLV
MFGLGGIYVE VLKDISFRLA PLSLADARDM IREVRSYMLL KGFRGEPAVN FQALERIILT
MSALAMDFPE IYEAEFNPVL AGEQGAIVAD VRLSLSS
//
