ID A0A0F7JUZ1_9GAMM Unreviewed; 663 AA.
AC A0A0F7JUZ1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:AKH19412.1};
GN ORFNames=AAY24_02555 {ECO:0000313|EMBL:AKH19412.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19412.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH19412.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19412.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP011412; AKH19412.1; -; Genomic_DNA.
DR RefSeq; WP_046858351.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7JUZ1; -.
DR KEGG; seds:AAY24_02555; -.
DR PATRIC; fig|1543721.4.peg.538; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000034410; Chromosome.
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; PS00866; CPSASE_1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000034410}.
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 588..663
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 663 AA; 71599 MW; 715AB37C772CBFA4 CRC64;
MFDKILIANR GEIACRVART ARRLGITTVA VYSEADADAM HVTLCDEAYL IGPAAAKESY
LRADKILAVA KASGAQAVHP GYGFLSENAE FAEACQAAGI VFIGPPAAAI IAMGSKSEAK
RIMSEAGVPL VPGYHGDDQS DERLRQEADA MGYPLLIKAT AGGGGKGMRV VEKAGDFLTG
LNAAKREAIA SFGDDKVLLE RYLLAPRHVE LQVFADTQGN AVHLFERDCS VQRRHQKVLE
EAPAPGMTPE LRDAMGEAAI NAAKAIGYVG AGTVEFLLDS DGKFYFMEMN TRLQVEHPVT
EMISGQDLVE WQLKVAAGEA LPLAQSELRI NGHAFEARVY AENPAREFLP ATGTLRYLQT
PETGPCVRVD TGVEQGDEVS VHYDPMIAKL IVWGEDRASA LHKLRAALAD YRIVGVTTNL
EFLSTLCALP AFGNAELDTG FIDKHEAELF PVTEPVSDDI LAIAALYELL VEQRDILQRQ
ARSNDPFSPW GSATGWRMNQ DSFHQLHWAS GEQQGSVVAH YRDGSFLLEL PGGDCLVSGE
LLENGDLLAD LAGRRFKVAV IKHDQELTIL HQGRSWQLLL SDPRLEALEG EGAGGSLVAP
MTGNVIAIHV QEGDAVKQGD AVMIVEAMKM EHTITAPADG TVKEVRFAVG DQVQDGEPLL
VIE
//
