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Database: UniProt
Entry: A0A437LGC9_9RHOB
LinkDB: A0A437LGC9_9RHOB
Original site: A0A437LGC9_9RHOB 
ID   A0A437LGC9_9RHOB        Unreviewed;       667 AA.
AC   A0A437LGC9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 9.
DE   SubName: Full=Acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:RVT84437.1};
GN   ORFNames=DXV76_12185 {ECO:0000313|EMBL:RVT84437.1};
OS   Rhodobacteraceae bacterium CCMM004.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2499834 {ECO:0000313|EMBL:RVT84437.1, ECO:0000313|Proteomes:UP000287438};
RN   [1] {ECO:0000313|EMBL:RVT84437.1, ECO:0000313|Proteomes:UP000287438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMM004 {ECO:0000313|EMBL:RVT84437.1,
RC   ECO:0000313|Proteomes:UP000287438};
RA   Zhang Z.;
RT   "Salalgibacter marinus gen. nov., sp. nov., isolated from a Synechococcus
RT   culture.";
RL   Submitted (JAN-2019) 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:RVT84437.1}.
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DR   EMBL; RZWH01000003; RVT84437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437LGC9; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000287438; 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; 3.30.700.40; -; 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; 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:UP000287438}.
FT   DOMAIN          1..456
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..322
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          585..663
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   667 AA;  69550 MW;  B1A9A15F05602012 CRC64;
     MIGTLLIANR GEIACRVIAT ARSMGVSTVA VHSDADAGAR HVEMADRAVR IGPAPVSESY
     LRADAILEAA RATGADAIHP GYGFLSENPD FVEAVEGAGL IFVGPPAAAI RAMGLKDAAK
     AAMQRAGVPV VPGYHGERQE PDFLAGEADA IGYPVLIKAR AGGGGKGMRR VDGPDDFAEA
     LEGARREAEA AFGDPACLIE KYVDTPRHVE IQVFADAHGN VVHLFERDCS LQRRHQKVIE
     EAPAPGMTPE VRAAMGAAAV EAARAIGYVG AGTVEFIADG SRGLRPGGFW FMEMNTRLQV
     EHPVTEAITG LDLVALQLRV AAGEPLPFAQ EDLRIDGHAF EARLYAEDAS RGFLPATGRL
     AHLRFPAATA FARGPVRVDS GVRPGDAITT HYDPMIAKLI VHGPDRAAAL RRLRHALAET
     QIVGTVTNRD FLAALAGHAG FAAGEVDTGL IARDQDALTA AAAPDAEVWA VAALAALGLP
     AEPPGRSPWD ALTGWRAWGP AVQNAVLIHS GTRTEVPVAF LGPGRFAVGA GQDAVALSAR
     CLEDGAVEIV CDGITRRLTV HRGTDAVWVL ADGGAHRFDL PDPLAAAAGA EAAADTVTAP
     MPGLVKRLAA TQGQAVTAGQ RLAVLEAMKM EHTLTAPRDG TVAEVLVSEG AQVSDGDPLI
     RLETADE
//
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