ID G7GU18_9ACTN Unreviewed; 700 AA.
AC G7GU18;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=accA {ECO:0000313|EMBL:GAB07093.1};
GN ORFNames=GOAMR_61_01910 {ECO:0000313|EMBL:GAB07093.1};
OS Gordonia amarae NBRC 15530.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB07093.1, ECO:0000313|Proteomes:UP000006023};
RN [1] {ECO:0000313|EMBL:GAB07093.1, ECO:0000313|Proteomes:UP000006023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB07093.1,
RC ECO:0000313|Proteomes:UP000006023};
RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
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:GAB07093.1}.
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DR EMBL; BAED01000061; GAB07093.1; -; Genomic_DNA.
DR RefSeq; WP_005191325.1; NZ_BAED01000061.1.
DR AlphaFoldDB; G7GU18; -.
DR STRING; 1075090.GOAMR_61_01910; -.
DR eggNOG; COG4770; Bacteria.
DR Proteomes; UP000006023; 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:UP000006023}.
FT DOMAIN 6..453
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 589..663
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 700 AA; 73666 MW; 83DE76E8EF7854B2 CRC64;
MTTVKPIRTV LIANRGEIAC RVITTLRRMG IRSVAVYSDA DANARHVAEA DVAVHIGPAA
ATRSYLDIDT IVDAARATGA DAVHPGYGFL SENQKFAAAL EAAGIIFIGP PAGAIATMGD
KITARAAVVE RDVPVVPGIS RPGLTDDDLI AAAPGIGFPV LIKPSAGGGG KGMHRVEDPA
ELPAALQRAR REAGSAFGDD SLFLEHFIDT PRHIEVQVLA DNHGNVIHLG ERECSLQRRH
QKVIEEAPSA LLDHETRTRI GQAACDAARS VGYSGAGTVE FIVSSKRPGD FFFMEMNTRL
QVEHPVTELV TGVDLVEQQI RVARGEVLSL TQDDIVLTGH AVEARVYAED PAAGFLPTGG
TISHLDEPGG PGVRVDSAMA PGLVVGSDYD PMLAKVIAHG GDREEAIERL DAALAHTRVL
GVVTNIDFCR YVLNRPEVTE ARLDTELLDR LVVDYAEPQP VPEALVLVGL CRTGTRESDV
WRSAVGWRIG GPAPVITRIA DGADAYTVSI VVDDAAESSL RGTATVTHDD GRDPWTSSIV
YHEADQGISR LIVDGVSQSW SAARVDDVWW VSGVPGTWRF TLARSVLDEA TDAHAGDLAS
PMPGTVVAVP AADGATVAAG EPVIVVEAMK MEHTLTAPVD GVVTLSAKAG DKVAAGQILA
TVTPSPVEAP PLVEVPPSLV EVPPSLVEAR GAQATSLETS
//
