ID C6KUV1_9BACT Unreviewed; 235 AA.
AC C6KUV1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:BAH89748.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:BAH89748.1};
RN [1] {ECO:0000313|EMBL:BAH89748.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Ohnuki T., Miyazaki K.;
RT "Functional screening of a metagenomic library for genes involved in
RT microbial degradation of aromatic compounds.";
RL Environ. Microbiol. 9:2289-2297(2007).
RN [2] {ECO:0000313|EMBL:BAH89748.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Koyama Y., Miyakoshi M., Miyazaki R., Yano H., Sota M.,
RA Ohtsubo Y., Tsuda M., Miyazaki K.;
RT "Novel organization of aromatic degradation pathway genes in a microbial
RT community as revealed by metagenomic analysis.";
RL ISME J. 0:0-0(2009).
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DR EMBL; AB266128; BAH89748.1; -; Genomic_DNA.
DR AlphaFoldDB; C6KUV1; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR011054; Rudment_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; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 1..227
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 27..98
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 235 AA; 25846 MW; BA8ADF29F8D98A4F CRC64;
MLHLGERDCS LQRRYQKMVE EAPAFGLAES LRQGMRDAAV ALARHIGYRS AGTVEFIVDV
ERNEFFFLEM NTRVQVEHPV TEMITGIDIV AAQLAIAAGE PLAIDQEDVV FSGHAVECRI
NAENPSRNFA PSPGRLAEWS PPEGPGIRID SHARPGYLVP PFYDSLVAKL IVHAGDRTEA
IARMQAALDQ FRVAGINTTI PFLKDVMAQP AYVEGKVNTT WLEGVAKEFM AAEAV
//
