ID A0A1H3ESV6_9PSED Unreviewed; 659 AA.
AC A0A1H3ESV6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Geranyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:SDX81054.1};
GN ORFNames=SAMN05216287_3833 {ECO:0000313|EMBL:SDX81054.1};
OS Pseudomonas kuykendallii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1007099 {ECO:0000313|EMBL:SDX81054.1, ECO:0000313|Proteomes:UP000243778};
RN [1] {ECO:0000313|Proteomes:UP000243778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-59562 {ECO:0000313|Proteomes:UP000243778};
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; FNNU01000006; SDX81054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3ESV6; -.
DR STRING; 1007099.SAMN05216287_3833; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000243778; 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; 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:UP000243778}.
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 581..655
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 659 AA; 71355 MW; E63489A4AAF50FDF CRC64;
MAAFDKILIA NRGEIACRVM RTAIELGYRT VAVYSEADAD ARHVELADEA VCIGPAQVNQ
SYLVIENIIA AAQKTGADAI HPGYGFLSEN ADFARACEAA GIVFIGPGVE AIHLMGSKRL
SKIAMLDAGV PCIPGYEGAD QDEANLAEQA ARIGYPLMIK ASAGGGGRGM RLVQDSGELI
AGLRTARSEA QNAFGNGELI LERALVQPRH VEIQVFGDRH GNVVHLGERD CSVQRRHQKV
VEESPCPVMT PALRQAMGDA AVKAAASVSY VGAGTVEFLL DANGEFFFLE MNTRLQVEHP
VTELVTGQDL VAWQIKVAEG QPLPLRQEQI QLSGHAMEVR LYAEDPAHGF LPQTGEVLRW
EPAEREGIRI DHGLREGQRI SPFYDPMLAK VIAYGATRDE ARRKLIRAVE DCVLLGVNGN
QRFLANLLRH PQFAAGRAST AFIAEHFADD ASLFPQRAAT GELACAAALL YQSHAQANRQ
RTGWRNAAQA TACFQLGQAE QRHRVELRVI EPGAQPQLLA QVGDARIALR LLDGDGRWAT
LEIDGVRRRQ AYHLAGDKLW LYGASGNLEL VDLTQAAADP SQAEGSTTLK APMDGAIVEV
LVSEGERVAK GQLLVVLEAM KMEHSLKAGL DGIVVRVQAN KGEQVKNRQM LVEIEPSEA
//
