ID A0A2U0H1N0_9MICO Unreviewed; 1204 AA.
AC A0A2U0H1N0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=uca {ECO:0000313|EMBL:PVW02718.1};
GN ORFNames=DEA06_15025 {ECO:0000313|EMBL:PVW02718.1};
OS Microbacterium sp. Gd 4-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2173179 {ECO:0000313|EMBL:PVW02718.1, ECO:0000313|Proteomes:UP000245623};
RN [1] {ECO:0000313|EMBL:PVW02718.1, ECO:0000313|Proteomes:UP000245623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gd 4-13 {ECO:0000313|EMBL:PVW02718.1,
RC ECO:0000313|Proteomes:UP000245623};
RA Spirina E.V., Kuleshov K.V., Rivkina E.M.;
RT "Genome sequencing and assembly of Microbacterium sp. Gd 4-13.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVW02718.1}.
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DR EMBL; QEIJ01000010; PVW02718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U0H1N0; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000245623; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase 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; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
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; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
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 Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000245623}.
FT DOMAIN 3..452
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 1121..1201
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1204 AA; 127696 MW; 0E7DFE94C7743764 CRC64;
MSGFDTLLVA NRGEIARRII RSARERGLRT VAVYSDADRA APHVREADTA VRLGPAPAAE
SYLRLDAVLE AAARTGAGAV HPGYGFLAEN AGAARAVEAA GLAWVGPTPD QLDAFGLKHT
ARELAAAAGV PLLPGSGVLE SRDAAVAAAE SIGFPVMLKA TGGGGGIGMR VCGDAGAVAE
AFDAVTRQAQ ASFGSSGLFV EKFVRPARHV EVQLFGDGAG RVAVLGDRDC SLQRRNQKVI
EEAPAPRLPD AVRAQLHATA AALAASVDYR SAGTAEFVYD PVAEAAYFLE VNARLQVEHP
VTEAVFGLDL VGLMLDLAAG GPEAVDPTLF DAPRRPNGHA VEARIYAEDP DRGNAPSTGL
VTGVRLPEGD GVRVDSWIEA GMDVTSYYDP LLAKVIAHAA TRDDALDLLH TSLADTRIDG
IVTGTGMLRE IAQHPRVRDA THDTGTLDGI GDPDPRIEVL EPGMMTTVQD LPGRLGYWQV
GVPPSGPMDA VSFREANLAV GNPPEAPGLE VTLTGPTLRL TAATTVCVTG APVDVTVDGA
AVALWEPVEV PAGGTLRIGA SAGPGIRTYV AIRGGIDVPA YLGSAATFTL GGFGGHGGRA
LVAGDVLRPV AAGPGAPGGA TPSERRPHIG REWRIGVTEG PHAAPEFFTR SDIDELYAAE
YTVQVNSART GVRLSGPQPE WARTDGGEAG LHPSNIHDTP YAVGALDFTG DTPIILGPDG
PSLGGFVCPA VVASGELWKI GQLRPGDSLR FVPVREADAA GLDSARSLGA PPLIGGGDGD
DGVVSVREAD VDATGVHRPR VTYRRDGDDN LLVEFGAQEL DLGLRMRVHA LQTRLAEHAP
RGILDVTPGI RSLQVHTDAS VLRASQLVGL LRELDDDLPP TSELVVPSRE VRLPLSWDDP
ATRLAIERYM AGVRDDAPWT PWNIEFIRRI NGLDSVDDVY RTVFDAQYLV MGLGDVYLGA
PVATPLDPRH RLVTTKYNPA RTWTAENSVG IGGAYLCIYG MEGPGGYQFV GRTVQVWNRF
RRGGLFADNP WALRFFDRIR WYPVSAEELL ELRAETDAGR GEFETSEGEF RLAEYETFLA
DNAAGISSFR DRQQRAFAEE RDRWREAGEF DRPVESDAVA TAPIEDPLPP GCIAVRAPFS
AAVWKVETEP GRSVAEGERM LVLEAMKMET TVSATQAGIV RDVLVRPGER VEAGQLLAVV
EVAR
//
