ID A0A3D9HSY0_9PROT Unreviewed; 671 AA.
AC A0A3D9HSY0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=3-methylcrotonoyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:RED52550.1};
GN ORFNames=DFP90_102573 {ECO:0000313|EMBL:RED52550.1};
OS Aestuariispira insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Aestuariispira.
OX NCBI_TaxID=1461337 {ECO:0000313|EMBL:RED52550.1, ECO:0000313|Proteomes:UP000256845};
RN [1] {ECO:0000313|EMBL:RED52550.1, ECO:0000313|Proteomes:UP000256845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8488 {ECO:0000313|EMBL:RED52550.1,
RC ECO:0000313|Proteomes:UP000256845};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) 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:RED52550.1}.
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DR EMBL; QRDW01000002; RED52550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9HSY0; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000256845; 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; 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:UP000256845}.
FT DOMAIN 1..450
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 594..669
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 481..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 72352 MW; 058C6CE8305D4F12 CRC64;
MFEKILIANR GEIACRVIET AQSMGIATVA VYSDADCGAK HVALADEAVH IGPAPVRESY
LLGERIIEAA KQTGAQAIHP GYGFLSENAG FADLCAKNDL IFIGPPADAI RAMGSKSQAK
EIMDKAGVPL VPGYHGDNQD PDFLAAEADK MGYPVLIKAS LGGGGKGMRL VEKAADFAAS
LESCKREAVN AFGDDHVLVE RFVTRPRHIE MQVFADSHGQ AVHLFERDCS VQRRHQKVLE
EAPAPGMNEE LRAEMGKAAT DAALAIGYQG AGTVEFIVET SEDGVPGAFF FMEMNTRLQV
EHPVTEMITG EDLVAWQLKV ASGMPLPKAQ SEITCTGHAL EARLYAEDPA NDFLPAIGRL
HHFKTPNAIA RIDSGVRAGD EVSMHYDPMI AKVITHGADR SEAIRRMVRA LEQTEVAGLV
TNRDFLKKAA GHPAFGSGLL DTSFIEKYET DLLPNEGEGA SVHDLAFAAL ALLRQRDRQA
RSEADHSADP WSPWGRTDNW RLNDTSNTDI RLQPMGASEP VMVHAEIDGQ DYHFRIADEV
LSFAAVREEG LDLTAQVNGV KAKRAVHLRE SALTVIGADR TQRLTLIDPM AAAGEEEGGS
GRMTAPMPGK ITAVKVNAGE SVEEGQALMV VEAMKMEHTI AAPHDGVVAE VRFAVGDQVA
EGDELISFEE V
//
