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Database: UniProt
Entry: A0A2V4MWJ4_9RHOB
LinkDB: A0A2V4MWJ4_9RHOB
Original site: A0A2V4MWJ4_9RHOB 
ID   A0A2V4MWJ4_9RHOB        Unreviewed;       668 AA.
AC   A0A2V4MWJ4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:PYC46854.1};
GN   ORFNames=DI396_12895 {ECO:0000313|EMBL:PYC46854.1};
OS   Litorivita pollutaquae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Litorivita.
OX   NCBI_TaxID=2200892 {ECO:0000313|EMBL:PYC46854.1, ECO:0000313|Proteomes:UP000248012};
RN   [1] {ECO:0000313|EMBL:PYC46854.1, ECO:0000313|Proteomes:UP000248012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSX-11 {ECO:0000313|EMBL:PYC46854.1,
RC   ECO:0000313|Proteomes:UP000248012};
RA   Hetharua B.H., Min D., Liao H., Tian Y.;
RT   "Oceanovita maritima gen. nov., sp. nov., a marine bacterium in the family
RT   Rhodobacteraceae isolated from surface seawater of Lundu port Xiamen,
RT   China.";
RL   Submitted (MAY-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:PYC46854.1}.
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DR   EMBL; QFVT01000009; PYC46854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V4MWJ4; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000248012; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000248012}.
FT   DOMAIN          2..444
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          121..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          590..664
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   668 AA;  71075 MW;  688C49B0B8F1EABB CRC64;
     MKIKTLLIAN RGEIACRIAR TARASGITPV GVHSDADANA LHVREIGHSV CIGAGPASES
     YLKIDAVIAA AKSVGADAIH PGYGFLAENS DFARAVEAAG MVFMGPTPDT LERFGDKASA
     KEAAVAASVP VISGAEGARS DPQEIAEEVR AMGLPVLLKA VGGGGGRGQR LVTDETTLVE
     DIEGALREAK STFGSEGLLL ERFLPEARHV EVQIAGDGKG HVVHLFERDC TLQRRHQKVI
     EEAPAWGLPR TLLDKIAQDA VRLGETLDYR GLGTVEFLVA GEEYFFLEVN PRIQVEHPVT
     EAITGLDLVA LHLRIAEGAG LGLVQDDLKI NGHAVEARLY AEDPAMQFAP STGTLTTLSL
     PEGLRIDSGV EEGDAVTPFY DPMIAKLVVH AADRETALAR LATALDHVAV EGVQTNRAFL
     TALARNPEFE QMQVHTRWID GRLDELTQAH TLSRPALWKA AAAILFVAAS RSDASTNPWT
     NRDTFTGWRL GLGGDAMEAG QHVTLTDAAD TSEEFRVGPI KAVDTYTVMS ENGDALTLAM
     REITPGRWRI SDGDDVFLID ARLHAGVIEM DTPEGRLVFR PAAPLDFAGG DAAGDRAVAS
     PLTGMIVEIK VADGQDVTEG DVIAVMESMK LEISIRATAA GIASNISVSN GDMVDRGQVI
     AEILPSEE
//
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