ID A0A0B2A139_9MICO Unreviewed; 669 AA.
AC A0A0B2A139;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=LK09_19560 {ECO:0000313|EMBL:KHK95300.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK95300.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK95300.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK95300.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-2014) 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:KHK95300.1}.
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DR EMBL; JTDK01000025; KHK95300.1; -; Genomic_DNA.
DR RefSeq; WP_039403421.1; NZ_JTDK01000025.1.
DR AlphaFoldDB; A0A0B2A139; -.
DR STRING; 1348253.LK09_19560; -.
DR Proteomes; UP000031030; 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: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:UP000031030}.
FT DOMAIN 6..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 585..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 669 AA; 70472 MW; 09B276464E28C2B4 CRC64;
MSDQTLFDTV LVANRGEIAR RVIRTLRRLG IRSIAVYSDA DVNAPHVHEA DEAVHIGGSA
ASASYLNIPA VLDAARQTGA DAIHPGYGFL SENAAFGAAC AEAGIVFIGP DARALEVMGD
KIRARDHVSG YGVPIVPGFS AAGMTDAEIG ERAEETGYPL LIKPSAGGGG KGMEVVRSAA
ELPGALATAR RVARASFGDD TLLLERLIER PRHIEVQVLG DGRGGAVHLG ERECTLQRRH
QKVIEESPSP VVDAQTRERL GAAACAAAAS VDYRGAGTVE FIVATARPDE FFFIEMNTRL
QVEHPVTEAV TGVDLVEQQL RIAAGLGADV PPGPVQLRGH AVEARVYAED PARGFLPATG
RVLQWDEAAG ARTDSAVEHG SVITADYDPM VAKVIAHAED RAGALAALDA ALAETVLLGV
DTNIAFLREL LAQPDVQAGT MDTGLIDRMP PFATPEPGEE SLRRAAQVVA LTARRWGSHE
TAGVWQSLPG WRSAAPAATT PVFLQDAGGH IHSVAAEGLQ EPSEPAAEAE EAEYAWFAMP
PDGVWMEMDD DTGTIWIHAE GLTSSFRVLT RRRAGELRRA SLAKDAAASD PDLPAPMPGA
VVAVHVTDGQ AVAAGDRILS IEAMKMEHPI TAPHEGTVRL HVSVGDQVQR DQVVAVVSIS
DPSSAPEGA
//
