ID F2R6W1_STRVP Unreviewed; 714 AA.
AC F2R6W1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Acetyl-CoA synthetase (ADP-forming) alpha and beta chains, putative {ECO:0000313|EMBL:CCA58740.1};
GN OrderedLocusNames=SVEN_5454 {ECO:0000313|EMBL:CCA58740.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA58740.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA58740.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA58740.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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DR EMBL; FR845719; CCA58740.1; -; Genomic_DNA.
DR RefSeq; WP_015036636.1; NZ_CP029197.1.
DR AlphaFoldDB; F2R6W1; -.
DR STRING; 953739.SVEN_5454; -.
DR GeneID; 69867525; -.
DR KEGG; sve:SVEN_5454; -.
DR PATRIC; fig|953739.5.peg.597; -.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_11; -.
DR OMA; MFIEVPP; -.
DR Proteomes; UP000006854; 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:UP000006854}.
FT DOMAIN 482..687
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 683..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 72202 MW; 3A532E67D507E853 CRC64;
MSDISALWEA ESIAVIGASE RPGALGRKPL DYLLRYGYKG RILPVNPRSP EILGVPAYPS
VKDAPGPVDL ALIMVSAERV LGAVDDCVAA GVKLAVIASS GFAETGEEGA RLQAEVVAKA
RAGGLRIIGP NCIGAVGYEN RVLATFSPLF GAESVPFEPG TLAFVSQSGA LGFGAASLAL
ERGLRPGWVV STGNDADVTA LEVLRELATV PDVTGLLGYL EDTPDIDTLR ALAGSGKPVA
LLKSGRTEAG GRAAASHTGA LATDDRVLDA ALRGLGIVRV DDIDELLDVA RVFESERRPA
GNRVAVVTTS GGSGILAADA VEAHGLQLST LEPRSKEALA EIVPAFGAID NPVDITATVL
SDPSLFDRSL DVLIADDTVD IIVAAFCVMA GPDVEKAVNA LSRAAAKGGK PILVARTGAD
FLAPDAPRDL REAGLPEYPT PARALRAAAA LWEVSRPRTL PDAPRPGTVP GPGSQATEPE
LKRLLAEAGI AVPKGRIAES AEDAVRAVTE VGGTAVLKAV VPGLLHKTEA GGVEIGVTTA
GAPAAHARLA ALGGQVLVEE LVGEGVELIV GVHTTDLGPV LTAGLGGIFT EVLDDVGHRL
LPLAPGEGAE LLAGLRGAKV LAGARGRAAV DVAAAAELLH KVAELAQDWP AGYALDLNPV
RVLPKGAVVL DAALGIETAT GAETAPGAET APGGDAASGV ETASGVAATE GAAR
//