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Database: UniProt
Entry: A0A0G9MVE7_9SPHN
LinkDB: A0A0G9MVE7_9SPHN
Original site: A0A0G9MVE7_9SPHN 
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}.
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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
//
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