ID A0A2T0LMM9_9PSEU Unreviewed; 594 AA.
AC A0A2T0LMM9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=B0I33_112215 {ECO:0000313|EMBL:PRX44337.1};
OS Prauserella shujinwangii.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=1453103 {ECO:0000313|EMBL:PRX44337.1, ECO:0000313|Proteomes:UP000238362};
RN [1] {ECO:0000313|EMBL:PRX44337.1, ECO:0000313|Proteomes:UP000238362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7125 {ECO:0000313|EMBL:PRX44337.1,
RC ECO:0000313|Proteomes:UP000238362};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRX44337.1}.
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DR EMBL; PVNH01000012; PRX44337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0LMM9; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000238362; 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:UP000238362}.
FT DOMAIN 6..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 517..593
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 499..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 62536 MW; 3D2F272D862C3337 CRC64;
MPEAASVTKV LVANRGEIAV RVIRAARDAG LSSVAVYADP DRDAPHVRMA DEAFALGGTT
AADSYLVFEK LLDAAARSGA DSVHPGYGFL SENADFAQAV LDAGLTWIGP SPQAIRDLGD
KVTARHIALK AGAPLVPGTK DPAKNADEIV AFAREHGLPV AIKAAFGGGG RGLKVARTLE
EIPELFESAT REAVAAFGRG ECFVERYLDR PRHVEAQVLA DKHGNVVVVG TRDCSLQRRH
QKLVEEAPAP FLTDEQRATI HASAKAICKE AGYSGAGTVE YLVGEDGTIS FLEVNTRLQV
EHPVSEETTG IDLVREQFRI AEGGTLPFTE DPVPRGHSIE FRINGEDAGR NFLPAPGTVT
RLVFPEGPGV RVDSGVETGS VIGGQFDSML AKVIVTGADR RQAIERSRRA LDEMVAEGLA
TVLPFHRAIL RDPAFVGDDS GFSVHTRWIE TEFDNTIEPF TAPAESSAAE QEAAPRQTVV
VEVGGRRLEV SLPGDLALGG GNGGGAAKAK PRKRGSGGKT AVSGDAVTAP MQGTIVKVAV
EDGQHVEAGE LIVVLEAMKM ENPVTAHKAG TVTGLAVETG SSVSQGAVLL EIKD
//
