ID A0A173LUZ7_9MICO Unreviewed; 591 AA.
AC A0A173LUZ7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=AUMI_11100 {ECO:0000313|EMBL:BAU98652.1};
OS Aurantimicrobium minutum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Aurantimicrobium.
OX NCBI_TaxID=708131 {ECO:0000313|EMBL:BAU98652.1, ECO:0000313|Proteomes:UP000243847};
RN [1] {ECO:0000313|EMBL:BAU98652.1, ECO:0000313|Proteomes:UP000243847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNC {ECO:0000313|EMBL:BAU98652.1,
RC ECO:0000313|Proteomes:UP000243847};
RA Nakai R., Fujisawa T., Nakamura Y., Nishide H., Uchiyama I., Baba T.,
RA Toyoda A., Fujiyama A., Naganuma T., Niki H.;
RT "Complete Genome Sequence of Aurantimicrobium minutum Type Strain KNCT, a
RT Planktonic Ultramicrobacterium Isolated from River Water.";
RL Genome Announc. 4:e00616-16(2016).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AP017457; BAU98652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A173LUZ7; -.
DR KEGG; amin:AUMI_11100; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000243847; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 3.40.50.20; -; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000243847}.
FT DOMAIN 3..447
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 512..588
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 591 AA; 63472 MW; 8AF84EB7BDECC105 CRC64;
MSRITKVLIA NRGEIAVRII RAARDYGIGS VAVYADQDRD ALHAKLADEA YALNGTTSAE
TYLVIDKLLA VARKSGANAV HPGYGFLAEN ADFARRVQDA GLIWIGPSPE AIEQLGDKVS
ARHVAEKVGA PLAPGTINPV SGAEEVLEFV DIHGLPVAIK AAFGGGGRGL KVARNREEVA
ELFDSATREA IAAFGRGECF VEKYLDEPRH VETQCLADAH GNVVVVSTRD CSLQRRHQKL
VEEAPAPFLT QEQTDELYRA SKAILKEVGY LGAGTCEFLI GKDGTVSFLE VNTRLQVEHP
VSEEVTGIDL VREQFRIAEG GVLDYPDPVV TGHSFEFRIN GEDGGRNFLP APGPVHVFRA
PGGPGVRVDS GVTAGDVISG SFDSLLAKLI VTGATREEAL ERSRRALDEF EVAGLPTVLP
FHRKIVRDPA FAPEGDKPFQ VYTRWIETEF VNDIEPWSGE AEETPSQAKR QHVTIEVDDR
RIEVSLPAKL LRANAADLAT QGPAPVRKVA SHAVGGASGS AVKAPMQATV VKIAVEEGQK
VVKGDLILVL EAMKMEQPVE AHKDGIISGV NAEVGQTVSS GHLLLNIDDV E
//
