ID C3KRA8_SINFN Unreviewed; 662 AA.
AC C3KRA8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=3-methylcrotonoyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:ACP22616.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:ACP22616.1};
GN Name=mccB {ECO:0000313|EMBL:ACP22616.1};
GN OrderedLocusNames=NGR_b11630 {ECO:0000313|EMBL:ACP22616.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234b {ECO:0000313|Proteomes:UP000001054}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP22616.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=14702322; DOI=10.1128/JB.186.2.535-542.2004;
RA Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., Raasch C.,
RA Liesegang H., Broughton W.J.;
RT "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. strain
RT NGR234.";
RL J. Bacteriol. 186:535-542(2004).
RN [2] {ECO:0000313|EMBL:ACP22616.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000874; ACP22616.1; -; Genomic_DNA.
DR RefSeq; WP_015887261.1; NC_012586.1.
DR RefSeq; YP_002823369.1; NC_012586.1.
DR AlphaFoldDB; C3KRA8; -.
DR KEGG; rhi:NGR_b11630; -.
DR PATRIC; fig|394.7.peg.1568; -.
DR HOGENOM; CLU_000395_3_1_5; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234b.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; 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, ECO:0000313|EMBL:ACP22616.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Plasmid {ECO:0000313|EMBL:ACP22616.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 1..450
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 582..657
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 662 AA; 71270 MW; D75ECCD2A9076A9F CRC64;
MFSKLLIANR GEIACRVIRT ARRLGIRTVA VYSDVDDDAL HVALADEAVR IGSATASDSY
LSAERILWAA RAVGADAIHP GYGFLSENAD FAAAVEAANM VFVGPSPNAI RAMGLKDAAK
ALMERSGVPV VPGYHGEEQE AGFLAAQAAE IGYPVLIKAR AGGGGKGMRR VERPEDFAPA
LEAARREAEA AFGDGSVLIE RYLTRPRHIE VQVFGDRHGN IVHLFERDCS LQRRHQKVIE
EAPAPGMTAE VRRAMGDAAV RAARAIGYAG AGTVEFIADV TNGLWPDQFF FMEMNTRLQV
EHPVTEAITG FDLVEWQLRV AAGEPLPKKQ SDIAIDGWSF EARIYAEDPA KGFLPAIGRL
KHLYFPDGAV RIDSGVRQGD MVTPYYDPLI AKLIVHGSNR SAALGQLQAA LKECRIGGTI
TNLDFLVRLT EEHDFRSGRP DTGLIDREIE RLTAPMAPDD EALALAAIVA TGVLEPAVTG
DPWSSLGYWQ IWGDGQRTIT VEHEGSRSTA TLKARGRDQF AVHAGSSTLP VLVLERFADG
ARLEVAGQKR VLRFARDGET LTLFLGGRNL VFHLPDSLSG GHSSEVADDE LIAPMPGLIK
LVRVGAGEAV AKGQPLVVME AMKMELTLSA TREGKVASVH VAEGAQVSEG TVLVKLDEEA
AE
//
