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Database: UniProt
Entry: A0A094L4E9_9GAMM
LinkDB: A0A094L4E9_9GAMM
Original site: A0A094L4E9_9GAMM 
ID   A0A094L4E9_9GAMM        Unreviewed;       658 AA.
AC   A0A094L4E9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KFZ29563.1};
GN   ORFNames=IDAT_00180 {ECO:0000313|EMBL:KFZ29563.1};
OS   Pseudidiomarina atlantica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ29563.1, ECO:0000313|Proteomes:UP000053718};
RN   [1] {ECO:0000313|EMBL:KFZ29563.1, ECO:0000313|Proteomes:UP000053718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ29563.1,
RC   ECO:0000313|Proteomes:UP000053718};
RA   Du J., Lai Q., Shao Z.;
RT   "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL   Submitted (JUN-2014) 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:KFZ29563.1}.
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DR   EMBL; JPIN01000001; KFZ29563.1; -; Genomic_DNA.
DR   RefSeq; WP_034728995.1; NZ_JPIN01000001.1.
DR   AlphaFoldDB; A0A094L4E9; -.
DR   STRING; 1517416.IDAT_00180; -.
DR   eggNOG; COG4770; Bacteria.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000053718; 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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          1..447
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          576..651
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   658 AA;  71786 MW;  21F88F636AA70A31 CRC64;
     MIAKLLIANR GEIACRIIRT ARHLGIRTVA VYSAADQQAQ HVQLADESVF IGPAPSAESY
     LVVDKIIAAA KQTGADAIHP GYGFLSENEA FADACASNNI IFVGPPTSAI AAMGSKSAAK
     SIMSEAEVPL VPGYHGNEQG LEKLLAEAEQ IGFPVLLKAA YGGGGKGMRI VESAKQFKEA
     LASAKREAQA AFGNDKMLVE KYLTKPRHVE IQVFCDQHGN AVYLAERDCS VQRRHQKVIE
     EAPAPALSER TRQAMGEAAV RAAQAIDYVG AGTVEFLLDT DNRFYFMEMN TRLQVEHPVT
     EMVTGQDLVA WQLQVAAGEP LPLSQDQVQL HGHAFEARIY AEDPHNDFLP STGVLHHLRT
     PNPAADVRID SGVVEGDEVS AYYDPMIAKL VVWGEDRATA LRKLLQALDS YRIAGVRTNI
     DFLRSIARHR DFAQANLTTR FIEKHEKVLF ADYTEQQIQD HAVLAALAEN LLERPSAGAD
     VWQQARGFRL NQPAQYALEL LYRDTPISVA LEQTGNGWRS QFDKRIWQAE LNGDCLSVSC
     DGHGYQVYVM QDAQSITVFS QSANLHFQRH LVADTLSQEP AAGSMTAPMN GTIVEVLVQP
     GDTVEAEQAL VIMEAMKMEY TIRAAHAGTV EQVFYGAGDL VSDGAELVSL STDTTGDA
//
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