ID Q39QG9_GEOMG Unreviewed; 668 AA.
AC Q39QG9;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase, biotin-containing alpha subunit {ECO:0000313|EMBL:ABB33505.1};
GN Name=mccA {ECO:0000313|EMBL:ABB33505.1};
GN OrderedLocusNames=Gmet_3292 {ECO:0000313|EMBL:ABB33505.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB33505.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB33505.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB33505.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000148; ABB33505.1; -; Genomic_DNA.
DR RefSeq; WP_004512516.1; NC_007517.1.
DR AlphaFoldDB; Q39QG9; -.
DR STRING; 269799.Gmet_3292; -.
DR KEGG; gme:Gmet_3292; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_7; -.
DR OMA; LVKWQLM; -.
DR Proteomes; UP000007073; Chromosome.
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:UP000007073}.
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 588..663
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 668 AA; 71535 MW; EEF2D5CBDBDD5CA1 CRC64;
MFDTILIANR GEIACRVIST ARRLGIRTVA VYSDTDADAL HVTMADEAYH IGLAPARESY
LRGDVILEVA ARSGAQAIHP GYGFLSENAE FAEACAKAGV VFIGPPTGAI RAMGSKSAAK
EIMEKAGVPL VPGYHGENQD PEFLGREAKR IGFPVLIKAS AGGGGKGMRA VREAVEFPDA
LASAKREAQA SFGDDRVLLE KYLTKPRHVE IQVFADTHGN AVHLFERDCS IQRRHQKVLE
EAPAPGMKPA LRKKMGEAAV AAASAIGYVG AGTVEFLLDE DGSFYFMEMN TRLQVEHPVT
EMITGQDLVE WQLQVAAGAP LPCRQKDLAI GGHAIEARIY AEDPAKDFLP SIGRLAHLRT
PAESANVRID TGVGQGGEVS IYYDPMIAKL IVWDTDRAGA LRRLQKALAD YQVVGVTTNI
GFLGSVAAHP AFAAADLDTG FIERHRTDLF PDPSLASDRT LALASLDVLL RRAAEAKRTA
LASADPYSPW HQTSGWRLNF DNHHDLHFLD GEKVVTITVH YRAEGYLLAL PGGDLLVRGE
LDAAGDILAD LGGARVKATV VRHGATLTIM KGGRSHTLAI HNPYALSGDE EGAGGRLTAP
MPGKVVAVMV EPGERVEKGR PLMILEAMKM EHTIAAPRDG LVARLNFTVG SLVSDGAELL
ALADEEGV
//