ID A0A0G9MVE7_9SPHN Unreviewed; 665 AA.
AC A0A0G9MVE7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:KLE34727.1};
GN ORFNames=AAW00_11275 {ECO:0000313|EMBL:KLE34727.1};
OS Aurantiacibacter luteus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE34727.1, ECO:0000313|Proteomes:UP000053464};
RN [1] {ECO:0000313|EMBL:KLE34727.1, ECO:0000313|Proteomes:UP000053464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA37 {ECO:0000313|EMBL:KLE34727.1,
RC ECO:0000313|Proteomes:UP000053464};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter luteus KA37.";
RL Submitted (APR-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:KLE34727.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBHB01000002; KLE34727.1; -; Genomic_DNA.
DR RefSeq; WP_047004375.1; NZ_LBHB01000002.1.
DR AlphaFoldDB; A0A0G9MVE7; -.
DR STRING; 1581420.AAW00_11275; -.
DR PATRIC; fig|1581420.6.peg.2302; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000053464; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053464}.
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 575..651
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 665 AA; 70937 MW; 0F872BE7E298B7E6 CRC64;
MIDKLLIANR GEIACRIIRT ARAMGVATVA VYSDADAKAL HVRQADEAVH IGPSPAAESY
LVGDKIIAAA KQTGADAIHP GYGFLSENAA FAQAVIDAGL IWVGPKPASI EAMGLKDAAK
KLMRAAGVPV TPGYEGEDQS VERLKAEAEA IGYPVLIKAV AGGGGKGMRK VDAPEDFEAA
LESCRREAKA SFGNDEVLLE KWITSPRHIE VQVFGDAHGN VVHLFERDCS LQRRHQKVIE
EAPAPGMDEA TREAICAAAV RAAKAVDYEG AGTIEFIADA SEGLRADRIF FMEMNTRLQV
EHPVTEEITG VDLVEWQLRV ASGAPVPLKQ EELSIKGHAI EARLYAEDPA KGFLPSTGQL
KHFNLGEDGR IETGVSRGSE ISPFYDPMIA KLIAFAGSRE NAIDDLIAIA ENVEVYPVKS
NAAFIAKLLD LPQFRAGELD TGLIERKIGG LIEAHAPHSV KLAAALWRAE TFEAARYDGD
HAMSPSGMFG FRLNAPSAPA RFALSVDGNG STVTLMPLDG GERWDVEIDG VREFDEIEYL
PTTHGPTAEV EPDCTILIFD RGNAHTVSFA RERGTGHASA ADGDISAPMP GKVIAVDVAE
GDTVTAGQRL LVLEAMKMEH ALTAPFDGVV AELSASEGAQ VQVEALLARI EQESVERSGA
DGMDA
//