ID A0A2P8AXY0_9ACTN Unreviewed; 583 AA.
AC A0A2P8AXY0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=accC_1 {ECO:0000313|EMBL:PSK65334.1};
GN ORFNames=B0E53_02705 {ECO:0000313|EMBL:PSK65334.1};
OS Micromonospora sp. MH33.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1945509 {ECO:0000313|EMBL:PSK65334.1, ECO:0000313|Proteomes:UP000240342};
RN [1] {ECO:0000313|EMBL:PSK65334.1, ECO:0000313|Proteomes:UP000240342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH33 {ECO:0000313|EMBL:PSK65334.1,
RC ECO:0000313|Proteomes:UP000240342};
RA Thatcher L.F., Myers C.A., O'Sullivan C.A., Roper M.;
RT "Draft genome sequences of Micromonospora sp. MH33 and MH99.";
RL Submitted (FEB-2017) 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:PSK65334.1}.
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DR EMBL; MUYZ01000069; PSK65334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8AXY0; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000240342; 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; 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, ECO:0000313|EMBL:PSK65334.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000240342}.
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 505..583
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 492..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 61036 MW; 7A27D9337D685934 CRC64;
MRKVLIANRG EIAVRVIRAC RDAGLASVAV YADSDRDALH ATLADEAYAL GGDTAADSYL
RIDKLIDVAA KAGADAVHPG YGFLSENADF AQAVIDAGLT WIGPTPQAIR DLGDKVTARH
IAQRAGAPLV PGTPDPVGNA DEVMAFAVDH GLPVAIKAAF GGGGRGLKVA RTMEEIPHLF
ESATREAVAA FGRGECFVER YLDQPRHVEA QVLADQHGNV IVVGTRDCSL QRRHQKLVEE
APAPFLTDAQ RRQIHDSAKA ICREAGYHGA GTVEYLVGAD GTISFLEVNT RLQVEHPVTE
ETAGIDLVRE QFRIADGEKL RFTEDPTPRG HSIEFRINGE DPGRNFLPAP GTITALRLPT
GPGVRVDTGI SAGDVIGGNF DSLLAKVIIS GETRTEALER ARRALDEMLV EGMATALPFH
RLVVRDEAFT AEPFTVHTRW IETGWNNTVP AFTAPAGAVE GPAGRETVVV EVGGKRLEVT
LPAGLGAGTA AAAPAAKKPA RRGGGAKAGA AASGDALTSP MQGTIVKIAV ADGDTVAEGD
LVVVLEAMKM EQPLHAHKAG TVSGLSAEVG AVITAGAAIC TIA
//
