ID A0A0J9E1E3_9RHOB Unreviewed; 650 AA.
AC A0A0J9E1E3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000313|EMBL:KMW56507.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:KMW56507.1};
GN ORFNames=AIOL_001461 {ECO:0000313|EMBL:KMW56507.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW56507.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW56507.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW56507.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-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:KMW56507.1}.
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DR EMBL; LFTY01000002; KMW56507.1; -; Genomic_DNA.
DR RefSeq; WP_049642387.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9E1E3; -.
DR STRING; 1675527.AIOL_001461; -.
DR PATRIC; fig|1675527.3.peg.1547; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000037178; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; 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; 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, ECO:0000313|EMBL:KMW56507.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000037178}.
FT DOMAIN 1..448
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 568..646
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 650 AA; 68443 MW; C7CA4910D0EC56B4 CRC64;
MFDKILIANR GEIACRIIET CRQMGVGTVA VYSDADAGAR HVALADQAVH IGAALPAESY
LRGARIIQAA LDSGAQAIHP GYGFLSENPD FVEAVEAAGL TFIGPSGQAI RAMGLKDAAK
ALMVEAGVPV VPGYHGAGQE DARLAAEADK IGYPVLIKAV AGGGGKGMRL VEAASEFGSA
LEAARAEAKG AFGNDAVLVE KFIQSPRHIE IQVFGDGTRA VHLFERDCSL QRRHQKVIEE
APAPGMPEAV RAAMGAAAVR AAEAIGYKGA GTVEFIVDGS GPLREDGFWF MEMNTRLQVE
HPVTEFITGL DLVAWQLLVA SGAPLPARQD ELAIDGHAFE ARLYAEDVPK GFLPATGRLT
HLSFPAGARA DTGVRAGDEI SPYYDPMIAK VIVHGSDREH ALQKLRQALA TTQVAGTVTN
LAFLRRLAAH PGFAKGAVDT GLIGRDLDAL TQEPVPCSKS RALAALGALG LGVAPRRAAE
GFALWQPMEH QARLDWRDEA ILARVQCQGG GYLVRLDGGE AAHHIRREGE DWWIDGGKVS
AELVVTGEGH VSVFWGNGYH FTVPDPLAVA AGDAAGGDVI EAPMPGLVKA VFVEAGQEVR
RGDRLAVLEA MKMEHTLTAP RDGDVSEVLV ATGAQVEAGA ALIQLTEDDA
//
