ID D0SC70_ACIJO Unreviewed; 663 AA.
AC D0SC70;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Putative acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:EEY96752.1};
GN ORFNames=HMPREF0016_01443 {ECO:0000313|EMBL:EEY96752.1};
OS Acinetobacter johnsonii SH046.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575586 {ECO:0000313|EMBL:EEY96752.1, ECO:0000313|Proteomes:UP000012047};
RN [1] {ECO:0000313|Proteomes:UP000012047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH046 {ECO:0000313|Proteomes:UP000012047};
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; GG704965; EEY96752.1; -; Genomic_DNA.
DR RefSeq; WP_005400593.1; NZ_GG704965.1.
DR AlphaFoldDB; D0SC70; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_6; -.
DR Proteomes; UP000012047; 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; 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; 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}; 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 579..657
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 663 AA; 73041 MW; 12AAADFF9F3469DB CRC64;
MFNKILIANR GEIACRVIRT AKKMGIATVA VYSDADAQAQ HVQQADEAIY IGESPAAQSY
LQIERIIQAA LDTGAEAIHP GYGFLSENDQ FANACQENNI VFIGPPVDAI LAMGLKATSK
SLMEKAGVPL TPGYHGTNQD PDFLKQQADA IGYPVLIKAS AGGGGKGMRL VDRGEDFLSH
LASCKSEARS SFGNDDVLVE RYVVQPRHIE VQVFGDTHGN YVHLFERDCS VQRRHQKVLE
EAPAPKMAES KLETMRQAAI DAARAVDYVG AGTVEFIVEQ DGTAYFMEMN TRLQVEHPVT
EMITGQDLVE WQLRIAFGEP LPKQQHELSI HGHALEARVY AEEPEKGFLP AIGKIHYLHY
PQQNEHVRVD SGIVEGDEIT TFYDPMIAKL IVWAKNREAA LTQMHHALSQ FHVDGLGNNI
AFLDRLVRSE SFKTANLDTN LIQREEAFLL QHNETASSEL IITAALIELL SRFASNKIAA
NPVWQAESLW RLNINASYAI KLALNDEEHK VYFSPAAKGF TAKYNGHSVF IQGELLEAHL
AKIECATSKK TYAYSSNAQG LTLYADGQSY KFAHIQPNFN TEDDASDANN LKAPMPGVIT
QVLVQNNSAV KKDDVLLTLE AMKIEYSIRA PHDGIVSAAY FQVGDQVKAG DELVEFSSLE
GAA
//
