ID A0A4Y9ET43_9SPHN Unreviewed; 662 AA.
AC A0A4Y9ET43;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:TFU06343.1};
GN ORFNames=EUV02_04950 {ECO:0000313|EMBL:TFU06343.1};
OS Glacieibacterium arshaanense.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingosinicellaceae; Glacieibacterium.
OX NCBI_TaxID=2511025 {ECO:0000313|EMBL:TFU06343.1, ECO:0000313|Proteomes:UP000297737};
RN [1] {ECO:0000313|EMBL:TFU06343.1, ECO:0000313|Proteomes:UP000297737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ1R-1 {ECO:0000313|EMBL:TFU06343.1,
RC ECO:0000313|Proteomes:UP000297737};
RA Li A.;
RT "Polymorphobacter sp. isolated from the lake at the Tibet of China.";
RL Submitted (FEB-2019) 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:TFU06343.1}.
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DR EMBL; SIHO01000001; TFU06343.1; -; Genomic_DNA.
DR RefSeq; WP_135245066.1; NZ_SIHO01000001.1.
DR AlphaFoldDB; A0A4Y9ET43; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000297737; 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 FunFam; 2.40.50.100:FF:000003; Acetyl-CoA carboxylase biotin carboxyl carrier protein; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.30.470.20:FF:000028; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 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; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_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}; Reference proteome {ECO:0000313|Proteomes:UP000297737};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 1..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 581..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 662 AA; 70380 MW; 6A22399DE9E1FB2E CRC64;
MHKLLIANRG EIARRIIRTA HRMGIDTVAL YSDADAGAPH VREATQAVHI GASPATESYL
DAAKILAAAK ASGADAVHPG YGFLSENAVF AESVIKAGLI WVGPSPAAMK AMGLKDTAKA
VMKKAGVPIT PGYQGTDQSL VRLERAAAQI GYPLLIKAVA GGGGKGMRSV NDAAAFAENL
LSCQREGAAS FGNPGVLLEK LITRPRHVEV QVFADKHGNV VHLFERDCSL QRRHQKVIEE
APAPGLSDNL RNMLGVAACA AATAIRYEGA GTVEFILDLD NTDKAGDPAF YFMEMNTRLQ
VEHPVTECIT GYDLVEWQLR VARGEMLPAH QDAIQVTGHA VEARFYAEDP ETGFLPSTGT
LKTLRFPAGQ GIRIDSGVEQ GSEISPYYDP MIAKVITHGA DRSAAIDRLV AALDGCVVEG
VKTNRAFLAR LVDHAAFRAG DIDTGFIARH GDDLATTEAA KPTLIALAAL ALAREGTTTS
AEGLFARLGN WRLNLPYERH IDLFGADNVA QTVVLRDEAG KQRLDGPGFR MLATSRWLDD
VNFEAELDGM LHRAVVLVGA DSVEVRVGAR VHRFARRALA ADARGLASDA RVAAPMPGRV
LALDVAVGDS VAVGDRLLVL EAMKMEHRLS AKLAGTIAAV HVAAGDQVAD GMLLVEIEGI
PA
//
