ID N1MXU9_9SPHN Unreviewed; 712 AA.
AC N1MXU9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Acetyl-CoA synthetase (ADP-forming) alpha and beta chains, putative {ECO:0000313|EMBL:CCW20337.1};
GN ORFNames=EBBID32_47120 {ECO:0000313|EMBL:CCW20337.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW20337.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW20337.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW20337.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW20337.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW20337.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCW20337.1}.
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DR EMBL; CAVK010000261; CCW20337.1; -; Genomic_DNA.
DR AlphaFoldDB; N1MXU9; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000013201; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000013201};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 505..558
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 712 AA; 73621 MW; 4235992DBBED6009 CRC64;
MTDMIDLDRP ASPTAAPSLD RLLRPGSVAI VGASDKPGAL GASVLANLVR QGFAGAIHLV
NPRRADIGGR PCVASVDDLP EGVDVAVLAI PRVGVLDTMR GLARRKVGAA VIFSAGFAED
GPQGLADQQE IARIARDAGM VVEGPNCLGL VNFRDNVSLT FIEMPEAKAQ GDRRVGIVSQ
SGAMAAVLAT TMIHRDVPLS CYISTGNEAA SGIEDYLTHL VDEPETAVIA MIAEHVRDPA
RFLAAARAAR AAGKQVVLLH PGRSAAGAAS AATHTGAMAG DHAVMAVHVE RAGVILVDSL
EELGDVAEML TRNASIGAGG TGVIAESGAF KAMMLDLSEA VALDLPTLTD ADSPALRAAL
PDFVPVTNPL DVTAQGLVDP GLYGRTLAAL VDDPRIATIL LTLIQTDTGT SHIKFAAVLD
ALASLRPDKP IIVGGVDEGG AVFADDLAAL RQAGVTYLPT AERAVRALAR ISAAAARDFT
TAPLDADPVA DLAQVGHSIP EYRSKAIMAD HGIAFPRFAM AHSVDEAIAA AETLGYPVVL
KAQSPDLPHK SDAGGVIINL KNREELAEGW DRLAANIAAS RPGLVLDGVL VEGMADKGVE
LIVGARNDPH WGATILVGFG GVAAELLHDV CLLPADLPRD AIIARIRTLR MAPLLDGFRG
APVMDIGAVA DVVQRLGRMV AATPAIREVD LNPVIVYPEG QGALALDALI SL
//
