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Database: UniProt
Entry: A0A329QJJ1_9ACTN
LinkDB: A0A329QJJ1_9ACTN
Original site: A0A329QJJ1_9ACTN 
ID   A0A329QJJ1_9ACTN        Unreviewed;       598 AA.
AC   A0A329QJJ1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=DPM12_15470 {ECO:0000313|EMBL:RAW11869.1};
OS   Phytoactinopolyspora halophila.
OC   Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC   Phytoactinopolyspora.
OX   NCBI_TaxID=1981511 {ECO:0000313|EMBL:RAW11869.1, ECO:0000313|Proteomes:UP000250462};
RN   [1] {ECO:0000313|EMBL:RAW11869.1, ECO:0000313|Proteomes:UP000250462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 96934 {ECO:0000313|EMBL:RAW11869.1,
RC   ECO:0000313|Proteomes:UP000250462};
RA   Tang S.-K.;
RT   "Phytoactinopolyspora halophila sp. nov., a novel halophilic actinomycete
RT   isolated from a saline soil in China.";
RL   Submitted (JUN-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:RAW11869.1}.
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DR   EMBL; QMIG01000018; RAW11869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A329QJJ1; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000250462; 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:UP000250462}.
FT   DOMAIN          4..447
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          123..320
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          514..593
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          491..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   598 AA;  63243 MW;  1C3313D876CF14C9 CRC64;
     MKRRVTRVLV ANRGEIAVRV IRACKDAGIG SVAVYADPDR DAPHARLADD AYALGGETST
     ETYLDISKII DIATRAGADA VHPGYGFLAE NAEFAEAVGT AGLTWIGPPP SAITALGDKV
     SARHIAQRAG APLVAGTPEP VSGADEVVAF AEQHGLPVAI KAAFGGGGRG LKVARTIDDI
     PELYDSAVRE AVASFGRGEC FVERYLDRPR HVETQCLADE HGNVVVVSTR DCSLQRRHQK
     LVEEAPAPFL TDAQNAELYR ASKAILREAG YVGAGTCEYL VGADGTISFL EVNTRLQVEH
     PVTEEVTGID LVREMFRIAD GEELGYDDPP VRGHSIEFRI NGEDAGRNFL PTPGPVTAFR
     PPSGPGVRLD AGVEQGSVIG QNFDSLLAKL VVTGADREQA IERSRRALAE FEVSGLATVI
     PFHRAVLDDD AFAPADPGKP FTVHTRWIET EWHNTIQPHP ATGAEDTAAP AERERVTVEV
     GGKRLDVVLP AGLGASSTGT GSSATTRKPV RRKSSTSGAT SATGDSLVSP MQGTIIKVVA
     EEGQKVTAGD PIVVLEAMKM EQPLNAHKSG TVTALDAEIG ATVSNGGIIC EIRDETAR
//
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