ID A0A2S7JYA9_9BURK Unreviewed; 679 AA.
AC A0A2S7JYA9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:PQA85229.1};
GN ORFNames=C5F52_04420 {ECO:0000313|EMBL:PQA85229.1};
OS Limnohabitans sp. TS-CS-82.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=2094193 {ECO:0000313|EMBL:PQA85229.1, ECO:0000313|Proteomes:UP000238850};
RN [1] {ECO:0000313|EMBL:PQA85229.1, ECO:0000313|Proteomes:UP000238850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS-CS-82 {ECO:0000313|EMBL:PQA85229.1,
RC ECO:0000313|Proteomes:UP000238850};
RA Shabarova T., Salcher M.;
RT "Limnohabitans TS-CS-82.";
RL Submitted (FEB-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:PQA85229.1}.
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DR EMBL; PTQX01000001; PQA85229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7JYA9; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000238850; 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 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; 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}.
FT DOMAIN 1..463
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 605..678
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 679 AA; 73098 MW; 85C87EB031FE774F CRC64;
MFKKILIANR GEIACRVAAT ARRMGIKTVA VYSDADAQAK HVQVCDEAVH IGGSAPKDSY
LRWERILQAA KDTGAQAVHP GYGFLSENED FAKACAAAGL VFIGPPASAI LAMGLKAESK
QLMEKAGVPL VPGYHAADQD PALLQREADR IGYPALIKAS AGGGGKGMRV VNSSAEFADA
LGSCKREAIN SFGDDAVLIE KYVQRPRHIE IQVFGDTHGN CVYLFERDCS VQRRHQKVLE
EAPAPGMTEA LRKQMGEAAV AAAKAVNYVG AGTVEFIVEQ TAYDKPESMK FFFMEMNTRL
QVEHPVTEAI TGLDLVEWQL RVASGEPLPL QQSDLRIHGH AIEARICAEN PDNNFLPATG
TLAVYRKPKC SSFALPSDAH AGVRIDDGVR EGDSISPFYD SMVAKLIVHG DTREQALARL
DEALSQTRIV GLTTNVQFLR HIIRTDSFST AKLDTALIQR EEKALFAQEP LGLALTAASV
VANTLHRERA LTGNDPFSRR DGWRAYGVAT RNFGFVFHGA SHNAVLTYAH DGSLQLNVAD
ADGDVSGVLA FREDGDALHI SFVQQQVRVQ VFHEAQGHED VAHVFAPQGA TRITMVDALA
HAGEAQEAGG RLTAPMPGKV VSFAVAAGDK VKAGQPLAVM EAMKMEHTIA APADGEVLEL
LYAPGDQVAE GEELLKLKV
//
