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
//