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Database: UniProt
Entry: H0QMH5_ARTGO
LinkDB: H0QMH5_ARTGO
Original site: H0QMH5_ARTGO 
ID   H0QMH5_ARTGO            Unreviewed;       603 AA.
AC   H0QMH5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   28-JUN-2023, entry version 40.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   Name=pccA {ECO:0000313|EMBL:GAB14026.1};
GN   ORFNames=ARGLB_054_00280 {ECO:0000313|EMBL:GAB14026.1};
OS   Arthrobacter globiformis NBRC 12137.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB14026.1, ECO:0000313|Proteomes:UP000003828};
RN   [1] {ECO:0000313|EMBL:GAB14026.1, ECO:0000313|Proteomes:UP000003828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB14026.1,
RC   ECO:0000313|Proteomes:UP000003828};
RA   Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL   Submitted (DEC-2011) 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:GAB14026.1}.
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DR   EMBL; BAEG01000054; GAB14026.1; -; Genomic_DNA.
DR   RefSeq; WP_003801954.1; NZ_BAEG01000054.1.
DR   AlphaFoldDB; H0QMH5; -.
DR   STRING; 1077972.ARGLB_054_00280; -.
DR   eggNOG; COG4770; Bacteria.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000003828; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000003828}.
FT   DOMAIN          15..458
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          134..331
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          522..602
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          508..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  63522 MW;  34A566B68086A142 CRC64;
     MSVKPEQSAG PVHSKLTKVL IANRGEIAVR IIRAARDEGI ASVAVYADPD RDALHVRLAD
     EAYALGGNTA AESYLVMDKL IEVARQSGAD AIHPGYGFLA ENAQFAAKVI DAGITWIGPS
     PEAISALGDK VQARHIAEKV GAPQVPGTAD PVASAEEILE FVDKFGLPVA IKAAFGGGGR
     GIKVARTREE IPELFDSAVR EATAAFGRGE CFIERFLDSP RHVETQCLAD AHGNVVVVST
     RDCSLQRRNQ KLVEEAPAPF LTEEQNRRLY ESSKAILKEA GYLGAGTCEF LVGQDGTISF
     LEVNTRLQVE HCVSEEVTGI DLVREQFRLA CGEELGYEDP EVRGHSFEFR ITGEDPGRNF
     MPAPGTVSTL KNPTGPGIRI DSGIEEGDVI SGNFDSMLSK LIVTGANRPQ ALQRARRALE
     EMVVEGIPTV IPFDLAVVSN PAFAPAEGPF SVHTRWIETE FVNDLPAWTP NGAAPEGEDA
     AERRTVVVEV GGKRLEVALP ASLGFGGAAA AGTKPAKSKK RSRTGGATAA AGGNALASPM
     QGTIVKVAVA DGDVVAEGDL VVVLEAMKME QPLTAHRAGT ITGLSAAAGQ TVAAGAVIAT
     IED
//
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