ID A0A0X3Y6R0_9GAMM Unreviewed; 661 AA.
AC A0A0X3Y6R0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KUM52511.1};
GN ORFNames=AR688_09440 {ECO:0000313|EMBL:KUM52511.1};
OS Rheinheimera sp. EpRS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1712383 {ECO:0000313|EMBL:KUM52511.1, ECO:0000313|Proteomes:UP000054239};
RN [1] {ECO:0000313|Proteomes:UP000054239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS3 {ECO:0000313|Proteomes:UP000054239};
RA Presta L., Bosi E., Fondi M., Maida I., Maggini V., Bogani P.,
RA Firenzuoli F., Chiellini C., De Pascale D., Palma F., Di Pilato V.,
RA Rossolini G., Mengoni A., Fani R.;
RL Submitted (NOV-2015) 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:KUM52511.1}.
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DR EMBL; LNQS01000009; KUM52511.1; -; Genomic_DNA.
DR RefSeq; WP_068234823.1; NZ_LNQS01000009.1.
DR AlphaFoldDB; A0A0X3Y6R0; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000054239; 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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 579..657
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 661 AA; 72849 MW; 8ADF462ADAC213EB CRC64;
MFRKILIANR GEIACRVIDT AHKLGIRCVA VYSEADANAR HVRMADEAYL LGPAPSKDSY
LRADKIIAIA KQSGAQAIHP GYGFLSENES FAKACDEAGV VFIGPPVGAI TAMGSKSAAK
DIMAKAGVPL VPGYHGDDQS DALLSKESER IGYPQLLKAA YGGGGKGMRV VWKKAEFADA
LASARREAKA GFGNDKMLIE RYLTKPRHIE IQVFADNHGN AVYLAERDCS IQRRHQKVIE
EAPAPNFSSE QRKAMGEAAV KAAKAIDYRG AGTVEFLFDE DGSFYFMEMN TRLQVEHPVT
EMITGQDLVK WQLLVAAGEK LPLAQDDIQL DGHAIEVRVY AEDPDNDFLP QTGKLTYLRQ
PEANRHVRVD TGVVENDEVS PFYDPMIAKL IVWDESRDRA IARMLRALDD YRIAGVTTNL
GFLTSLTEHP AFKAAELDTN FINQHQHTLF APANKENNQA LVLAALYILQ QQKAPQTSCN
SFSPWQFSHG WRMNETPTVE IALQHGEHKT LLKVQQLQQH YVVDVEGQQL CCTAELNGDE
LSAVLGDHRT KVRVSRYADT ISVFIKHQRY DFIYQTEVTT EVEGTDHAGS LTAPMNGTIV
AVMAKAGSTV NAGDTLVIME AMKMEYSIKA PKNGVINEVF YAAGDLVKDG AELVDFSPEE
A
//
