ID A0A2U1WR01_9PROT Unreviewed; 668 AA.
AC A0A2U1WR01;
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:PWC54341.1};
GN ORFNames=TSO221_08880 {ECO:0000313|EMBL:PWC54341.1};
OS Azospirillum sp. TSO22-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=716789 {ECO:0000313|EMBL:PWC54341.1, ECO:0000313|Proteomes:UP000245126};
RN [1] {ECO:0000313|EMBL:PWC54341.1, ECO:0000313|Proteomes:UP000245126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSO22-1 {ECO:0000313|EMBL:PWC54341.1,
RC ECO:0000313|Proteomes:UP000245126};
RA Jang J., Ishii S.;
RT "Comparative genome analysis of Azospirillum sp. strains.";
RL Submitted (JUL-2015) 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:PWC54341.1}.
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DR EMBL; LGQZ01000028; PWC54341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1WR01; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000245126; 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; 3.30.700.40; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000245126}.
FT DOMAIN 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 589..665
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 668 AA; 71738 MW; 71B3F88BAC09C658 CRC64;
MFSKILIANR GEIACRVIRT ARRMGLKTVA VYSDADAEAM HVAMADEAYR IGPAPVRESY
LKIEAILDVA KRSGAEAIHP GYGFLSENER FAEACAAAGV VFIGPPPSAI RAMGGKSEAK
ALMETAGVPL VPGYHGADQD PALLRAEAER IGWPVLIKAS AGGGGKGMKV AASAAEFDAQ
LASAKRESAA AFGDDRVLIE KYLERPRHVE IQVFADGQGR CVYLFERDCS IQRRHQKVIE
EAPAPNLPSE VRRRMGEAAV AAAKAIGYVG AGTVEFLYDP AQGGFYFMEM NTRLQVEHPV
TEMITGQDLV EWQLRVASGE PLPVGQDDLT IHGHAIEARL YAEDPDRDFL PQTGTLEHLG
FPPCGPHVRV DAGVRAGDAI SVHYDPMIAK LIVWDVDRAS AVRRMRAALG ATQVVGLATN
VRFLEGLASH PAFLGADLDT RFIERHRADL LPEPAAAGPR ALALAALGVL LDRERTAREA
AAASADPWSP WVRTDGWRLN EEARDTLTFR ENGEDRLVGV VYRRDGYRLE LPGGESVTAG
GEFNPGGTLE ADLDGVRLSS VWVRQGADIT VFHPGGSHRL TLVEPLTGAL DQDVPGGRVA
APMPGKIIAL LAEPGSRVEK GQPLLVLEAM KMEHTLKAPS AGTLTAYRCA VGDQVEEGND
LVSFEAEG
//
