ID A0A1I3CIX8_9PSED Unreviewed; 662 AA.
AC A0A1I3CIX8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Geranyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:SFH74303.1};
GN ORFNames=SAMN05216206_0092 {ECO:0000313|EMBL:SFH74303.1};
OS Pseudomonas guineae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=425504 {ECO:0000313|EMBL:SFH74303.1, ECO:0000313|Proteomes:UP000243606};
RN [1] {ECO:0000313|Proteomes:UP000243606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24016 {ECO:0000313|Proteomes:UP000243606};
RA Varghese N., Submissions S.;
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; FOQL01000001; SFH74303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3CIX8; -.
DR STRING; 425504.SAMN05216206_0092; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000243606; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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:UP000243606}.
FT DOMAIN 3..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 578..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 662 AA; 71236 MW; 39A4559E3596BC6B CRC64;
MPAFNKILIA NRGEIACRVM RTAQDLGYRT VAVYSEADAD ARHVQQADEA VCIGPAQVNQ
SYLVIDNIIA AAQKTGADAI HPGYGFLSEN ADFARACQAA GIVFIGPTVE AIHLMGSKRL
SKIAMLEAGV PCIPGYEGAD QDEETLIREA GRIGYPLMIK ASAGGGGRGM RLVHQASELA
EKIRTARSEA QNAFGSGELI LERAVIQPRH VEIQVFGDSQ GNIVYLGERD CSVQRRHQKV
VEEAPCPVMT PQLRQAMGEA AVKAAASVSY VGAGTVEFLL DQSGEFFFLE MNTRLQVEHP
VTELITGQDL VAWQIRVAEG QPLPLKQDDI RLTGHAMEVR LYAEDATQNF LPQTGTALRW
EPALRDGIRI DHGLIEGQVI SPFYDPMLAK VIAYGATREE ARRKLVRAVE DCVLLGVNGN
QRFLANLLSH PEFAAGNATT AFIAEHFADD PSLSPQAPAA GELAAAAALL FQQSANARAH
QGGLAGWRNA GSAPWRFVLK HGEQSFNVAL DVLSDGTQPK LLATLGEQQI SLTLLASDSR
WATLEVDGIR QRLAYHLEGD NLWLYGHNGN LHLSDITHQP VSSAAGAGSG SVKAPMDGAI
VEVLVEEGAS VSKGQLLVVL EAMKMEHPLK ASIDGVVRRI GVSRGDQVKN RQLLVDIEAS
DA
//
