ID A0A1I3PUK2_9BRAD Unreviewed; 669 AA.
AC A0A1I3PUK2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:SFJ24987.1};
GN ORFNames=SAMN05216525_12124 {ECO:0000313|EMBL:SFJ24987.1};
OS Bradyrhizobium sp. Gha.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855318 {ECO:0000313|EMBL:SFJ24987.1, ECO:0000313|Proteomes:UP000199284};
RN [1] {ECO:0000313|EMBL:SFJ24987.1, ECO:0000313|Proteomes:UP000199284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gha {ECO:0000313|EMBL:SFJ24987.1,
RC ECO:0000313|Proteomes:UP000199284};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; FOQM01000021; SFJ24987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3PUK2; -.
DR STRING; 1855318.SAMN05216525_12124; -.
DR Proteomes; UP000199284; 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 9..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 586..663
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 669 AA; 72115 MW; 09261C4676DD31A8 CRC64;
MDRSKLYRRF RTLLIANRGE IACRVIRTAR AMGLRTVAVY SEADRDALHV EMADEAVLIG
PPAAAESYLV IEKIVEACRK TGAEAVHPGY GFLSENAEFA QACFDAGLVF VGPTAEMMTA
MGSKSGSKAL MEKAGVPLVP GYHGEAQDDA TLSKAADKIG FPILVKASAG GGGRGMRIVR
SAAELAPAIV SAKREAKAAF GDDRMLIEKY VDNPRHIEVQ IIGDSHGNLL SLFERECTLQ
RRHQKVIEEA PSPTLNAAQR ETVCAAARKA AGAVNYVGAG TIEFVSDGKD VFFIEMNTRL
QVEHPVTELI TGIDLVEWQL RVAFGEALPL KQDEIRLNGH AVEARVYAES PTKNFMPSVG
KISTWRLPAE TGGLRIDAGY REGDTVSPYY DAMLAKMIAW APTRDVAIDR LNRGLEDSDV
RGIVTNIPFL SALITHPKVR ANAIDTGFIE RELTGLTQAS PAPGELELCA AVAAIVNEER
QVAQSEPSSP WQTFGWQPVG RRQRSFAFRV GHGPEQKIAL NYGHGLSTLV IGDRELAFTV
APKHGGFDLT LDGVKTSVAA VICGHELYLR TRNGRFDLHW VDPFGGETEE QTGADKIAAP
LPGTVVAVLA EEGAKLDKGA PILTLEVMKM EQTLRAPYAG VLTSIKCKVG DIVQEGVELA
VVEPSGGVT
//
