ID   A0A1Y0ND96_9BURK        Unreviewed;       896 AA.
AC   A0A1Y0ND96;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha {ECO:0000313|EMBL:ARV20644.1};
DE            EC=6.2.1.5 {ECO:0000313|EMBL:ARV20644.1};
GN   Name=sucD_2 {ECO:0000313|EMBL:ARV20644.1};
GN   ORFNames=AEP_03726 {ECO:0000313|EMBL:ARV20644.1};
OS   Curvibacter sp. AEP1-3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Curvibacter.
OX   NCBI_TaxID=1844971 {ECO:0000313|EMBL:ARV20644.1, ECO:0000313|Proteomes:UP000196261};
RN   [1] {ECO:0000313|EMBL:ARV20644.1, ECO:0000313|Proteomes:UP000196261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AEP1-3 {ECO:0000313|EMBL:ARV20644.1,
RC   ECO:0000313|Proteomes:UP000196261};
RA   Foret S., Pietschke C., Fraune S.;
RT   "Curvibacter sp. AEP1.3.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP015698; ARV20644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0ND96; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000196261; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
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; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000182; GNAT_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; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000313|EMBL:ARV20644.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196261}.
FT   DOMAIN          487..523
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          732..896
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   896 AA;  96462 MW;  EC1EC77F5B31DD21 CRC64;
     MEKHYLSPLF TPQSIIVFAG QVDAPEQLPP QARMLVAALQ AQTFTGLLRF LDIHSTGTLA
     DLAQSRADLA VIALPPEDLT AALEIAGRIA CKAAVIVSSG ISAELAASLA KIAKREGVQL
     LGPNSLGLQR PQLQLNASLA GPLAQRGPLA LVSQSGALAS SMLDWAANNA VGFSTVVSLG
     PHTSVDLAHV LDFLANDAQT QSIVVYMEGI SDARRFMSAL RMAANAKPVV VLKAGRRPAG
     NEAAQTHSGA IVGSDDVFDA ALRRAGAVRV RSFVELFSAA KCLASRYRPV GKRLALVTNG
     GGPGVLAADW INELQLELGR LSATTAETLK PLLPPLASLT DLIDLSEEAD AEHFKAALDA
     AGKDRGVDGV LAIYSPKAGH DASAVAIALA EVKKTIGKPL LSCWMGDSTV NAARGILKAA
     EIPSFRTPEA AVGAFGNIAS FYQNQLLLQQ TPPPLSTLAK PDIEGARLVI ESVLAERRKV
     LTEMESKTLL SAFHIPVTRT ILARSANEAM MIATQLGFPA VLKIDSPDIS HKSDVGGVAL
     NIMNATGVRD TYNDMMQTVK RLRPDARING VTVQSMVRSR HGREIYIGLV TDDPFGPVIA
     FGAGGTMIEL INDRAMELPP LNQFLARRLI ERSRVAETLG EWRGNAPANI DLLEQILLRI
     SEMVCELPQL REMDINPIIV DEHGALAVDA RIVIDNAPQG VSSRVHNYNH LSILPYPAQY
     EQLWPMRGGG EYTVRPVQPD DAQMLQDLVQ GLSKESRYFR FVSSMHELPP AMLARFTLID
     YDREMALVAI HKTRTAGEDG EMLETERIIG VSRYVTNPDK SSCEFSLVVA DDFAGKGLGS
     RLMMSIMDVA RDKGLSEIEG LVLTHNPGML KLMRSLGFTV KTFEEDADFK LVSHPL
//