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Database: UniProt
Entry: A0A147IKP9_9SPHN
LinkDB: A0A147IKP9_9SPHN
Original site: A0A147IKP9_9SPHN 
ID   A0A147IKP9_9SPHN        Unreviewed;       617 AA.
AC   A0A147IKP9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:KTT95105.1};
GN   ORFNames=NS355_16965 {ECO:0000313|EMBL:KTT95105.1};
OS   Sphingomonas yabuuchiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=172044 {ECO:0000313|EMBL:KTT95105.1, ECO:0000313|Proteomes:UP000073923};
RN   [1] {ECO:0000313|EMBL:KTT95105.1, ECO:0000313|Proteomes:UP000073923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS355 {ECO:0000313|EMBL:KTT95105.1,
RC   ECO:0000313|Proteomes:UP000073923};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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:KTT95105.1}.
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DR   EMBL; LDTF01000114; KTT95105.1; -; Genomic_DNA.
DR   RefSeq; WP_058746751.1; NZ_LDTF01000114.1.
DR   AlphaFoldDB; A0A147IKP9; -.
DR   PATRIC; fig|172044.3.peg.308; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000073923; 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; 3.30.470.20; 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}.
FT   DOMAIN          1..451
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..322
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          536..612
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   617 AA;  65165 MW;  F69F1143F394712E CRC64;
     MMKSLLIANR GEIACRIIRT AREMGLRTIA VYSEADAQAL HVRLADEAIL IGPAPARESY
     LDAARILAAA RESGAEAIHP GYGFLSENAE FAESVIAAGL VWVGPNPDSI RAMGLKDAAK
     ARMIAAGVPV TPGYLGEDQD PDRLAAEAEA VGYPVLIKAV AGGGGKGMRR VDDPAAFSEA
     LASCRREAAA SFGDDRVLIE KYILSPRHIE VQVFGDRHGQ VVHLFERDCS LQRRHQKVIE
     EAPAPGMDAA TREAVCGAAV RAAQAVDYVG AGTIEFIADA SEGLRADRVW FMEMNTRLQV
     EHPVTEAITG VDLVEWQLRV AAGESLPIAQ GDLAIHGHAI EARLYAEDPA KGFLPAIGTL
     EVFDLGDDPA IRIDTGVEEG AEITPWYDPM IAKVIAHGDT RDAAREALAD ALDEAVIWPV
     RTNAGFLVQA LDHPDFASGQ VDTGLIAREG EALMPPTEPS EEALAEAAAA LIGQDGLSGF
     RLNAAPRRSA RFLLDGRPIT VDFSEAGEVP LAPTDEVLIS EGGQSWSFTR WRADGLAAGG
     AGDGAILSPM PGRIIAVAVT EGQAVSTGQP LVTMEAMKME HVLTAPFDGV VTDLKAETGG
     QVAEGIALVR IVAEDAA
//
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