ID A0A0D5AHI2_9NOCA Unreviewed; 720 AA.
AC A0A0D5AHI2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acetyl-CoA synthetase (ADP-forming) alpha and beta chains {ECO:0000313|EMBL:AJW42218.1};
GN ORFNames=NY08_4215 {ECO:0000313|EMBL:AJW42218.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW42218.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW42218.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW42218.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP010797; AJW42218.1; -; Genomic_DNA.
DR RefSeq; WP_045198360.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5AHI2; -.
DR STRING; 1564114.NY08_4215; -.
DR KEGG; rhb:NY08_4215; -.
DR PATRIC; fig|1564114.4.peg.4159; -.
DR HOGENOM; CLU_007415_3_1_11; -.
DR Proteomes; UP000032410; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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.
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..547
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 720 AA; 75412 MW; 7CE8D8FBFB5F00BC CRC64;
MTKATVQGMD LRALFEPRSI ALIGATDKSP WSLNTYQNIK DSGFGGSVYL VNPTSPIVHG
ERTFDSIAGL PEVVDLIFVM VPTTVVLQTL RVAVEHGVRA AVILTAGFGE TGAVGQQMED
EIIDFARSSG LTVLGPNGNG FINAAENITP YGLPIGRPLI EGTVGFVLQS GALASSVLQF
AQSRNVGVSF LTAMGNESLM SVTDVMNYLV DDPNTSVIAL FLESVRDPVE FRRIALRALR
AGKPIVALKI GRSVLGARAA LAHTGALVGD NAVIDAAFEQ MGVIRVRSLE DLITTAGLMA
SLGGGLPGPR IGVVTPSGGA SEIIADRAED EGLVLPGFSE ETTTRLGEIV PAFATVQNPL
DVTGYVVIDR TLMRRSLAVV AQDPNVDFAV LLSELPRVPA ADPSLTMTAY GESARNIRET
AVPTVVLSTV LTDVTEYGRS VADATEFPHV VGGIEHGLTA LGNAVRWSAL RAAASATPEE
LDPVVVPVDF DTEPTGIWTE YRSSELLSRN GIPVIPSSLV GSVEEAQERA AAYGYPVVLK
AVADGLGHKS DIGGVRLDLR SADDVAEAYN SVLATLADAG ATGTAALIQP QRPSNGLEML
VGVVRDPVWG LTLAVGLGGV WVEVLADAAI RVLPVGVADV RDAIESLRGI ALLRGTRGSE
PVDIDALATC VAEIGDFAYR LGDRLQALEI NPLMVRGGEC EALDALITWS ETGSETEAVS
//
