ID A0A1M3DI53_9SPHN Unreviewed; 635 AA.
AC A0A1M3DI53;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:OJV34664.1};
GN ORFNames=BGO24_12850 {ECO:0000313|EMBL:OJV34664.1};
OS Sphingomonas sp. 67-36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV34664.1, ECO:0000313|Proteomes:UP000183964};
RN [1] {ECO:0000313|EMBL:OJV34664.1, ECO:0000313|Proteomes:UP000183964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=67-36 {ECO:0000313|EMBL:OJV34664.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJV34664.1}.
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DR EMBL; MKSU01000002; OJV34664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3DI53; -.
DR STRING; 1895849.BGO24_12850; -.
DR Proteomes; UP000183964; 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..449
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 555..631
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 635 AA; 67784 MW; A84F18D484AFB986 CRC64;
MIRSLLIANR GEIACRIIRT ARAMGVRTVA VYSDADANAL HVRQADEAVH IGPSPARESY
LVGERIIAAA KTTGAEAIHP GYGFLSENAD FAQAVIDAGL VWVGPKPASI RAMGLKDAAK
KLMQEAGVPT TPGYLGEDQS PERLKAEADA IGYPVLIKAV AGGGGKGMRR VDAGEDFADA
LLSCQREAAS SFGDDRVLLE KYILSPRHIE VQVFGDAHGN AVHLFERDCS LQRRHQKVIE
EAPAPGMDPA TRAAICAAAV KAARAVDYVG AGTIEFIADA SAGLSADRIW FMEMNTRLQV
EHPVTEEITG VDLVEWQLRV ASGEPLPKRQ EELSINGWAI EARLYAEDPA KGFLPSTGRL
EHLALPDDAR VETGIEAGDT ISPFYDPMIA KLVTAAATRD AAIAGLARAC REVECTPVRT
NAWFLARLLD QPAFGSGDIT TAFISDHLET LIAPPRPSDT LLEYAADDAV FDQTHLSDAY
DLPQDFLVER FGFRLNAPSQ RTVRLSVDGE CRQVAVSDDA LHDNSYRPSV IDGPRRIYFE
DGAAFSVAPP RFDASATGGA ADGAILSPMP GRVIAVEAAA GDSVTKGQKL LTLEAMKMEH
SLVAPFDGTV AELNAATGGQ VSEGALLARI ERAEG
//
