ID A0A178MUM3_9PROT Unreviewed; 667 AA.
AC A0A178MUM3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:OAN53981.1};
GN ORFNames=A6A05_09215 {ECO:0000313|EMBL:OAN53981.1};
OS Magnetospirillum moscoviense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1437059 {ECO:0000313|EMBL:OAN53981.1, ECO:0000313|Proteomes:UP000078543};
RN [1] {ECO:0000313|EMBL:OAN53981.1, ECO:0000313|Proteomes:UP000078543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BB-1 {ECO:0000313|EMBL:OAN53981.1,
RC ECO:0000313|Proteomes:UP000078543};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) 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:OAN53981.1}.
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DR EMBL; LWQU01000123; OAN53981.1; -; Genomic_DNA.
DR RefSeq; WP_068498651.1; NZ_LWQU01000123.1.
DR AlphaFoldDB; A0A178MUM3; -.
DR STRING; 1437059.A6A05_09215; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000078543; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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:UP000078543}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 586..661
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 667 AA; 71694 MW; ABFA6831A7AAE01D CRC64;
MFDKILIANR GEIAVRVIRT AKRLGIRTVA VYSEADANAL HVRLADEAIL IGPAAAAESY
LVADKILAAA KATGAQAIHP GYGFLSENAC FAEACAAQGV TFIGPPAGAI RAMGSKAESK
RLMEAARVPM VPGYHGADQS DAVLTQAAGE IGYPLLVKAS AGGGGKGMRV VRAEAELASA
IAGARREAKA SFGDDSLLLE RYLDHPRHVE IQVFCDRLGN GIYLFERDCS AQRRHQKVIE
EAPAPLLPDE IRQAMGEAAV QAAKAVSYEG AGTVEFLFQD GQFYFIEMNT RLQVEHPVTE
MITGQDLVEW QLLVAAGRPL PLGQHELIRK GHAFEARLYA EDPAKDFLPA TGRLVHLVPP
LSSPHVRVDT GVVEGDEVTA FYDPMIAKLI VWDEDRDSAL RRLRRALADY EVAGLVTNIS
FLAAIAGHPA FAAFEMDTGF IDRHRADLIP ASRPVPAAAL AFAAAALLLD REDHAAAAAA
RSGDRWSPWH QTGGWRMNDD NHHDFRLIDA DAVRLVTVHF RTDGWEVDLD GGTMRVRGAG
RQGRRITAEL DGERRSASVV TDGFDITVLL DGASWRLKLD DPSAKAADQD GPGSLAAPMT
GRVVQVLVAA GDRVERGQPL MVVEAMKMEH TIAAPADGTV KEVLYAVGDQ VADGAELLAF
DADEAKK
//
