ID W0A329_9SPHN Unreviewed; 697 AA.
AC W0A329;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=NX02_02985 {ECO:0000313|EMBL:AHE52354.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE52354.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AHE52354.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AHE52354.1,
RC ECO:0000313|Proteomes:UP000018851};
RA Ma T., Huang H., Wu M., Li X., Li G.;
RT "Completed genome of Sphingomonas sanxanigenens NX02.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP006644; AHE52354.1; -; Genomic_DNA.
DR AlphaFoldDB; W0A329; -.
DR STRING; 1123269.NX02_02985; -.
DR KEGG; ssan:NX02_02985; -.
DR PATRIC; fig|1123269.5.peg.577; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_2_5; -.
DR Proteomes; UP000018851; Chromosome.
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:UP000018851};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 489..540
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 697 AA; 71730 MW; 5D6635673AB21A89 CRC64;
MTMPNLSRLL TPRSVVIVGA SPTPGALGNS VLQNLERHRF AGEIHLINPK RDEIGGRPCL
KSIDQLPEGV DAAVLAIPGG AVLGAVEALA ARGVGAAIIF SAGFAEGGEE GLAAQAAVAR
IAAEHGMVIE GPNCLGMVNY AAGVPLTFVE APVLDLAGRP SVGIVSQSGA MAVVLGTTLM
AKGLGITVSV STGNEAASGV EDYVEHLIDD PATPAIGMIV EQFRKPARFL ALAERARAAG
KAIVLLHPGT SSAARESAAT HTGAMAGDWQ LMKTKVERAG VILVDSLEAL GDVLELVTRA
KPVRRGGTAV LTESGAFKAL TLDLAEQIGL ALPPMDGATA SAMRAAIPDF IPVSNPMDLT
AQALVDPDLY RRTLEPLLAD DNFAALVFGI IQTDEATSAR KFPAIIDAVT RLAPDKPVIF
AGLDDGAPVP AAYIERLRAI GVPYFPSPDR AFRALRHLAR AAERDVSRAG AEPVTLDLPS
GVIPEYRAKE LLAPLGIPFP KGGFAASAEE AGAVAARVGY PVAIKAQAAA LSHKSDAGGV
ILNIADAAAL DAAWARLYDN VAAYDPGIAL DGALIEAMGK RGTELIVGAR NDPEWGPVIL
VGFGGVTAEL LHDVRLLPVD LTADAIAAEL RLLKQGALLD GYRGSPALDV EAVATLIAAL
GRALAGTPAI REVDLNPVVV YPKGEGAVAL DALILAE
//
