ID A0A1H3GDB1_9ACTN Unreviewed; 585 AA.
AC A0A1H3GDB1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Biotin carboxyl carrier protein /biotin carboxylase {ECO:0000313|EMBL:SDY01266.1};
GN ORFNames=SAMN05444365_101372 {ECO:0000313|EMBL:SDY01266.1};
OS Micromonospora pattaloongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=405436 {ECO:0000313|EMBL:SDY01266.1, ECO:0000313|Proteomes:UP000242415};
RN [1] {ECO:0000313|Proteomes:UP000242415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45245 {ECO:0000313|Proteomes:UP000242415};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNPH01000001; SDY01266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3GDB1; -.
DR STRING; 405436.SAMN05444365_101372; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000242415; 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; 3.40.50.20; -; 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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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:UP000242415}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 510..585
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 490..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 61408 MW; 09591A9EF79B427E CRC64;
MRKVLIANRG EIAVRVIRAC RDAGLASVAV YADSDRDALH ATLADEAYAL GGETAAETYL
RIDKLLDVAA RSGADAVHPG YGFLSENADF AAAVIDAGLT WVGPTPQAIR DLGDKVTARH
IAQRAGAPLV PGTPDPVAGP DEVIAFAEAH GLPVAIKAAF GGGGRGLKVA RTLDEIPELF
ESATREAVAA FGRGECFVER YLDQPRHVEA QVLADHHGNV IVVGTRDCSL QRRHQKLVEE
APAPFLTPEQ RAEIHESAKA ICREAGYHGA GTVEYLVGRD GTISFLEVNT RLQVEHPVTE
ETAGIDLVRE QFRIAAGDKL RFSADPTPRG HSIEFRINGE DPGRNFLPAP GTVTALRLPT
GPGVRVDTGI SAGDVIGGNF DSLLAKVIIT GETRAEAIER ARRALDEMIV DGMATALPFH
RLIVRDPAFT TEPFSVHTRW IETEFDNTVP PFTAAAGSTE TAQERETVVV EVGGKRLEVS
LPAGFGAGTA TAAAGTGARK PARRGSASKA GGAASSDALT SPMQGTIVKI AVAEGDQVQE
GDLVVVLEAM KMEQPLNAHK AGVVTALSAE VGAVVTAGAA ICTIA
//
