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Database: UniProt
Entry: D0S2X5_ACICA
LinkDB: D0S2X5_ACICA
Original site: D0S2X5_ACICA 
ID   D0S2X5_ACICA            Unreviewed;       664 AA.
AC   D0S2X5;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Putative acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:EEY77792.1};
GN   ORFNames=HMPREF0012_00661 {ECO:0000313|EMBL:EEY77792.1};
OS   Acinetobacter calcoaceticus RUH2202.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=575585 {ECO:0000313|EMBL:EEY77792.1, ECO:0000313|Proteomes:UP000005126};
RN   [1] {ECO:0000313|Proteomes:UP000005126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RUH2202 {ECO:0000313|Proteomes:UP000005126};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; GG704949; EEY77792.1; -; Genomic_DNA.
DR   RefSeq; WP_003651154.1; NZ_GG704949.1.
DR   AlphaFoldDB; D0S2X5; -.
DR   HOGENOM; CLU_000395_3_1_6; -.
DR   Proteomes; UP000005126; 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; PS00866; CPSASE_1; 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}.
FT   DOMAIN          1..447
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          581..657
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   664 AA;  73798 MW;  F44A5D5C9B300CB9 CRC64;
     MFEKILIANR GEIACRVIRT AKKLGIATVA VYSDADANAQ HVKLADEAIY IGQSPATQSY
     LQADRIIQAA IDTGSQAIHP GYGFLSENDQ FALACQQHNI CFIGPPVDAI LAMGLKATSK
     ALMEKAGVPL TPGYHGTNQD ADFLKQQADQ IGYPVLIKAS AGGGGKGMSL VERSEDFLHA
     LASCKREAKS SFGNDDVLIE RYVIQPRHIE VQVFGDTHGN YVHLFERDCS VQRRHQKVLE
     EAPAPQMPSE KLDAMRQAAI DAARAVDYVG AGTVEFIVEQ DGTAYFMEMN TRLQVEHPVT
     EMITGEDLVE WQLRVAYGEP LPKLQNELQI HGHALEARIY AEEPEKGFLP AIGKIDYLHY
     PTQNQYVRVD SGIVEGDEIT TYYDPMIAKL IVWGKNREAA LIQMQHALGQ FHVDGLGNNI
     AFLEKIVRSD SFKQAKLDTN LIQREQNFLF SPEDIKPELV VAAAFIEFLS KLNNNNSSSQ
     KQLWQAQPLW RLNIAYQHSI KLNYLNQNIQ IKFASNEQGF TAEYNGQSYP ISGQLIDAHT
     ASVQIGGTKQ KLSFNQSQQG ITLFQNGQSY KFAYIRQDFN QADSQADEGH LKAPMPGVVT
     QVLVSANHSV KKDDILMTLE AMKMEYTIRA PKDGVIVDSY FQVGDQVKAG DELVEFQPAQ
     EEVA
//
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