ID A0A1X9MBK7_9BACI Unreviewed; 707 AA.
AC A0A1X9MBK7;
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 synthetase subunit alpha {ECO:0000313|EMBL:ARK29980.1};
GN ORFNames=BkAM31D_08965 {ECO:0000313|EMBL:ARK29980.1};
OS Halalkalibacter krulwichiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK29980.1, ECO:0000313|Proteomes:UP000193006};
RN [1] {ECO:0000313|EMBL:ARK29980.1, ECO:0000313|Proteomes:UP000193006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM31D {ECO:0000313|EMBL:ARK29980.1,
RC ECO:0000313|Proteomes:UP000193006};
RA Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP020814; ARK29980.1; -; Genomic_DNA.
DR RefSeq; WP_066152054.1; NZ_CP020814.1.
DR AlphaFoldDB; A0A1X9MBK7; -.
DR STRING; 199441.BkAM31D_08965; -.
DR KEGG; bkw:BkAM31D_08965; -.
DR Proteomes; UP000193006; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000193006}.
FT DOMAIN 27..63
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 707 AA; 76879 MW; 624CA84ECC30A9F0 CRC64;
MGRNNIEEPT VVTEKGSNGF LMEYEGAEIL CEYGLPVAKS KLARTEEEAI ELANTIGYPI
VLKGMSRDIV HKTEAGIVKV NITNQTQLIK SFNEVLTNAS NYNSEAKMAG VLVQEMASKG
IELIIGIKKD PIFGHQLVIG FGGTLVEIMK DFSMRMMPVS KEDIAEMIKE LKSYPIIEGY
RGQQGINKQK LIDICLGLNN LVAERPEIEE LDLNPIMFSG NEAAICDVRI LVGNDQKNEV
SNRDLTNVKY MLNPRSIAVI GASTNEKKNG GRLFRYIVEN NFDGELYPIN PGATEIKGYK
AYPSLKEVPG EIDLACIIVG AKHVPQVMEE CIAKGIKAAI VYSSGFAEIG EEGQALQERL
LSLAEEGNIR VLGPNSIGIA SPSKNIYTAF GAALESKVKV PGNIGFISQS GAMGSALLSR
AWEQGAGFSR WVSVANEADL TIPDFIEVLA EDELTNVITV FMEGIKDAKA FKKATEKAFQ
QKKPVLVFKT GRSSVGKRAV QSHTGSIAGD DAVFSAAFKK YGALRIDHIE ELIDVSRAFN
IQRLPKGNRV GVLTASGGAC SVIADLCSEK GLEVPELKES INEIKELIPS FGSAQNPVDV
TAEVIAKPEM FKKVMETLTR DSNIDGVIVM LTTNADPGAT VIAQAILDVF NESDKPIVVG
RLGAEAIATQ AMDFYQKNAF PVYSTPEKVV NVMDYLVRYS KISQEKK
//
