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Database: UniProt
Entry: A0A418NSU6_9SPHN
LinkDB: A0A418NSU6_9SPHN
Original site: A0A418NSU6_9SPHN 
ID   A0A418NSU6_9SPHN        Unreviewed;       623 AA.
AC   A0A418NSU6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 11.
DE   SubName: Full=Acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:RIV85995.1};
GN   ORFNames=D2V07_10535 {ECO:0000313|EMBL:RIV85995.1};
OS   Aurantiacibacter zhengii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=2307003 {ECO:0000313|EMBL:RIV85995.1, ECO:0000313|Proteomes:UP000286576};
RN   [1] {ECO:0000313|EMBL:RIV85995.1, ECO:0000313|Proteomes:UP000286576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V18 {ECO:0000313|EMBL:RIV85995.1,
RC   ECO:0000313|Proteomes:UP000286576};
RA   Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA   Xu X.-W.;
RT   "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT   sediment.";
RL   Submitted (AUG-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:RIV85995.1}.
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DR   EMBL; QXFL01000004; RIV85995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418NSU6; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000286576; 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; 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:UP000286576}.
FT   DOMAIN          1..449
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          543..619
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   623 AA;  66377 MW;  143B30FFB3CA4EB2 CRC64;
     MISKLLIANR GEIACRIIRT AREMGVATVA VYSDADARAL HVRQADEAVH IGPSPAAESY
     LVGEKIIAAA KQTGADAIHP GYGFLSENAG FAQAVIDAGL VWVGPKPASI DAMGLKDAAK
     TLMQDAGVPV TPGYLGKDQS VERLKKEADA IGYPVLIKAV AGGGGKGMRK VDRAEDFEAD
     LQSCRREAKA SFSNDEVLLE KWITSPRHIE VQVFGDSHGN VVHLFERDCS LQRRHQKVIE
     EAPAPGMDEA TREEICAAAV RAAKAVDYEG AGTIEFIADA SEGLRADRIF FMEMNTRLQV
     EHPVTEEITG VDLVEWQLRV ASGEAIPLKQ DELVINGHAI EARLYAEDPS SGFLPSTGPL
     DHFDLGHAGR IETGVEEGDV ISPHYDPMVA KLVAWGETRD EAIDELAAIA ESVEIWPVKT
     NAAFLANALL DDDFGEAELD TGFIERKLDT LVADAEPDDT IWQAAADFTL MAAMDEDVPS
     ALGFRLNAAP RIAATLGFKG EMRTVIASGK QDAAHATGFV EDARTVVFAD GQSFEFARDA
     RGTGAAAAAD GAILAPMPGK VITLDVAEGD SVTAGQRLMV LEAMKMEHSL TAPFDGTVTQ
     LSASEGAQVQ VEAVLAVVQP AED
//
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