ID A0A0P0LW58_9BURK Unreviewed; 689 AA.
AC A0A0P0LW58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:ALK90446.1};
GN Name=accA1_1 {ECO:0000313|EMBL:ALK90446.1};
GN ORFNames=L103DPR2_00022 {ECO:0000313|EMBL:ALK90446.1};
OS Limnohabitans sp. 103DPR2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678129 {ECO:0000313|EMBL:ALK90446.1, ECO:0000313|Proteomes:UP000063254};
RN [1] {ECO:0000313|EMBL:ALK90446.1, ECO:0000313|Proteomes:UP000063254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103DPR2 {ECO:0000313|EMBL:ALK90446.1,
RC ECO:0000313|Proteomes:UP000063254};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-2015) 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; CP011834; ALK90446.1; -; Genomic_DNA.
DR RefSeq; WP_055359198.1; NZ_CP011834.1.
DR AlphaFoldDB; A0A0P0LW58; -.
DR STRING; 1678129.L103DPR2_00022; -.
DR KEGG; lim:L103DPR2_00022; -.
DR PATRIC; fig|1678129.3.peg.22; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000063254; 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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000063254}.
FT DOMAIN 1..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 613..689
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 689 AA; 74131 MW; B0A109C1B7AB7115 CRC64;
MFKKILIANR GEIACRVAAT AQRMGIQTVA VYSDADANAK HVAACDEAIH VGGAAPKNSY
LRWEAIIEAA KATGAQAIHP GYGFLSENEA FAEACAKAGL VFIGPPASAI QAMGLKAESK
QLMEKAGVPL VPGYHGADQN PELLKREADR IGYPVLIKAS AGGGGKGMRA VEKSEDFAEA
LASCQREAQN SFGDQAVLIE KYVQRPRHIE IQVFGDTQGN CVYLMERDCS VQRRHQKVLE
EAPAPGMSEA LRKQMGEAAV AAARAVNYVG AGTVEFIVEQ RDNPSTGQVD MNFFFMEMNT
RLQVEHPVTE AVTGLDLVEW QLRVASGEPL PLKQDQIKLI GHAIEARICA ENPDNNFLPA
TGHLQVYKKP AHTAFERGTV RFDDGVRQGD TISPYYDSMV AKLIVHGDTR EQALALLDQA
LAQTQVVGLS SNVQFLRHVV HSPSFAEARL DTALIPREAD VLFNQERVGM NVAAAAVVAH
TLHQEQSKQG HDPFSKSDAW QSHAETSRRF PLEFAGETHT AWLLYGHDGQ MQLTWGDAAG
PGAKGAHDEF SFTAVQSAGH HASNALNVTW QGQRVTSEVV LQAGKPGQPA ELAHVFTAHG
ATRIRLINPL AHAEGAQDEK GGLTAPMPGK VVSFAVKAGE KVKAGQTLAV MEAMKMEHTI
AAPKDGEVTE LLYAPGDQIA EGAELLKLA
//
