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Database: UniProt
Entry: A0A417XSE6_9ACTN
LinkDB: A0A417XSE6_9ACTN
Original site: A0A417XSE6_9ACTN 
ID   A0A417XSE6_9ACTN        Unreviewed;      1846 AA.
AC   A0A417XSE6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|EMBL:RHW23235.1};
GN   ORFNames=D0Z08_30880 {ECO:0000313|EMBL:RHW23235.1};
OS   Nocardioides immobilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=2049295 {ECO:0000313|EMBL:RHW23235.1, ECO:0000313|Proteomes:UP000283644};
RN   [1] {ECO:0000313|EMBL:RHW23235.1, ECO:0000313|Proteomes:UP000283644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AB 2017083 {ECO:0000313|EMBL:RHW23235.1,
RC   ECO:0000313|Proteomes:UP000283644};
RA   Li C., Wang G.;
RT   "Genome sequencing of Nocardioides immobilis CCTCC AB 2017083 for
RT   comparison to Nocardioides silvaticus.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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:RHW23235.1}.
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DR   EMBL; QXGH01000053; RHW23235.1; -; Genomic_DNA.
DR   OrthoDB; 3754062at2; -.
DR   Proteomes; UP000283644; Unassembled WGS sequence.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866:SF126; BIOTIN CARBOXYL CARRIER PROTEIN; 1.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000283644}.
FT   DOMAIN          4..458
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          127..325
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          578..661
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1562..1845
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          662..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1528..1558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1846 AA;  198662 MW;  A85A79C8D78EE779 CRC64;
     MTVSFERIAI VNRGEAAMRF IHAARDLRAA GERIETVALY TDVERNARFV READEAYPLG
     PASARPYLDL ALLERALVET AADAVWVGWG FVAEEPAFVE LCDRLGVTFI GPSAEAMRRL
     GDKIGAKLLA EEVGVPVAAW SGGPVETLRD ALTAAEAIGY PMMLKASAGG GGRGIRMVTS
     PAELEEAYQR TRDEAERAFG SGVVFLERLV TGARHVEVQV IGDGHGTAWA LGVRDCSVQR
     RNQKVLEESA SPLLTAEQAD DLKASAERLA VAVGYQGAGT VEFLYQPGEK AFAFLEVNTR
     LQVEHPITEI TTDFDLVKAQ VHVARGGRLD DQPRPAESGH AIEARLNAED PDRDFAPSPG
     RVARLELPSG PGVRVDTGLA EGDTIPADFD SMIAKVIAYG RDRDEALARL RRAMSETTVV
     IEGGTTNKSF ILDLLDQPEI VSGAPAWADT AWIDRVRGEG RLTSQAHSGT ALVVAAIEAY
     DEQRRVEVDR LLETGHGGRP QVQHKVGQPT DLKLRGTTYK VTALQTGPGR YRVTIAAGSV
     VETADVEIAR IDEVHSRLLV NGRRHRIVSA THGPTHLVEV DGVTHRVGRD EGGVLRSPAP
     ALVVATPAAV GDEVAAGAPV LVLESMKMET VIQAPFAARV RELLAVTGSQ VETGAPLVRL
     EPVGDDGAEE SPQPADAAPA LDLPHDDMER TARQRADRHL ADLAALVQGY DVPRDDRVAA
     LRSYLVAREE LRAAGEDVIA GEAELLALFT DFAELSRNRP AGEELRTELK VHSSREHFHT
     FLRSLDTERG GLPEGFRQRL EQVLSRYGVA DLERTAVLEE AVFRIFLALQ RPAESVEVVT
     ALLQRWIGEA PPSEGPDGNV RELLERLKQA TQLRFPAVGD LARSVRFRWF DQPLVDEERT
     SVLAGVRDEV AALAADPQVP DRADRIDALA VIPEQIVRFL AERVERGASS GEWDDEPMLE
     VLIKRHYRDF DLHGASASHH DGRPFAVADY VLDERPTRLV TTVGTVAELA EGSDLVAGLR
     TELAARPEGT KAVLDLYLHW PLAPESIAAG RDELAAVLSG LGLAQDARRV TVAVCPGEGR
     PVDYFTFRPD GSHGVEEDEL VHGVHPMVGR RLNLWRLRNF HVTRIEAPDD VLLYECVARE
     NPADRRLVAL AQVRQLAVVH DEEGRVTALP HAERAVENCL EAIRRARTAR GAAGAKLDLN
     HVWVQVWPVV EADIAQLTGL QQKITPLTDG AGIAEVLAQG RVAGPDGTAT PIAIRFHARP
     GAGVVSSIEA PPTELLQPLD DYDSKVLRAR RRGLVYPYEL EAIVAGDGGT LVEHDLDDAG
     ALVPVDRPRG LNKAGILVTV ASTPTALHPE GVTRVVLCGD PTKALGAVSE PECSRVIAAL
     DLAERMGVPV EWFALSAGAR ISMDSGTENM DWVAAALRRI VEFTQAGGEI NVVVAGINVG
     AQPYWNAEAT MLMHTKGILV MTPDSAMVLT GKQSLDFSGG VSAEDNFGIG GYDRVMGPNG
     QAQYWAPDLS GACDVLMAHY EHTYVAPGES RPRDAATSDP ADRDVTTYPH SDPGSDFTTV
     GQIFSPVSNP DRKKAFDIRT VMRALADQDH ATLERWAGMA DADTTVVFDA RLGGHPVCLL
     GIESKPVPRR GFPPTDGPDV YTAGTLFPRS SKKAARAINA ASGNRPLVVL ANLSGFDGSP
     DSMRNLQLEY GAEIGRAIVN FRGPIVFCVV SRYHGGAFVV FSKALNPQMT VLALEGSFAS
     VIGGAPAAAV VFAGEVDKRT AADPGVTKLE AAIADASPSE RGPLVVELAE LKRALRAEKI
     SEVAAEFDGV HDIHRAVSVG SVDAVIAPER LRPEIIAVIE RGLGEL
//
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