ID F5XWY2_RAMTT Unreviewed; 676 AA.
AC F5XWY2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Candidate Acetyl/propionyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:AEG91743.1};
GN OrderedLocusNames=Rta_06650 {ECO:0000313|EMBL:AEG91743.1};
OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS TTB310).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG91743.1, ECO:0000313|Proteomes:UP000008385};
RN [1] {ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA Barras F., Heulin T.;
RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG91743.1, ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RX PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA Vermeglio A., Achouak W., Heulin T.;
RT "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL PLoS ONE 6:E23784-E23784(2011).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000245; AEG91743.1; -; Genomic_DNA.
DR RefSeq; WP_013899976.1; NC_015677.1.
DR AlphaFoldDB; F5XWY2; -.
DR STRING; 365046.Rta_06650; -.
DR KEGG; rta:Rta_06650; -.
DR PATRIC; fig|365046.3.peg.681; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_3_4; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000008385; 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:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000008385}.
FT DOMAIN 1..466
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 597..674
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 676 AA; 72460 MW; 41F2BA57F671BF72 CRC64;
MFQKILIANR GEIACRVAAT ARRLAVGTVA VYSDADARAK HVAACDEAVH IGGSAPRDSY
LRWERIIEAA RATGAQAIHP GYGFLSENEE FAQACADAGL VFIGPPASAV QAMGLKAQSK
QLMEKAGVPL VPGYHGANQD AAFLQDQAGR IGYPVLIKAS AGGGGKGMRA VEKAADFEAA
LASCKREAAG SFGDDAVLIE KYVQRPRHIE IQVFGDTHGN CLWLFERDCS VQRRHQKVLE
EAPAPGMAPE LRRRMGEAAV AAARAVDYVG AGTVEFIVEQ REGGKMDFFF MEMNTRLQVE
HPVTEAITGL DLVEWQLRVA AGEPLPLKQD QLRMHGHAIE ARICAENPDN NFLPATGTLQ
VYRTPPCAEF LHPLPLGEGG GEGRRARVDS GVREGDAISP YYDSMIAKLI VHGADRAEAL
ARLDRALAQT HIVGPATNVQ FLRQVVRSES FAKADLDTAL IQREAPSLFH RRSMPLPLAA
AAAVARTLLD EKAQEGRDPF SRRDGWRSHG VATRRFEFDF DGERAKAELS YLHDGGLFLA
VGDAAGPLVV DTDGSACIDI RFAGLRERVW VYAEGETDHV FGGRGAATIV SVDLLAHAGE
GQAETGRLTA PMPGKVVSFA VQAGDAVRKG QALAVMEAMK MEHTIAAPAD GTVAELLYGP
GDQVAEGAEL LRLAAT
//
