ID A0A286GL23_9PROT Unreviewed; 454 AA.
AC A0A286GL23;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:SOD96228.1};
GN ORFNames=SAMN05421508_105221 {ECO:0000313|EMBL:SOD96228.1};
OS Caenispirillum bisanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD96228.1, ECO:0000313|Proteomes:UP000219621};
RN [1] {ECO:0000313|EMBL:SOD96228.1, ECO:0000313|Proteomes:UP000219621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 140 {ECO:0000313|EMBL:SOD96228.1,
RC ECO:0000313|Proteomes:UP000219621};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OCNJ01000005; SOD96228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GL23; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000219621; 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 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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}; Reference proteome {ECO:0000313|Proteomes:UP000219621}.
FT DOMAIN 2..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 454 AA; 47881 MW; 29A600D96170B85E CRC64;
MAIRRLFIAN RGEIAVRVVR SAKALGIETV QAHSEADADM LAVRLADRAV CIGPAAAKHS
YLNIEAVVGA AREAGCDAVH PGYGFLAENA AFAEAVEAAG MIFVGPSPDT IRTMGDKAAA
RAAAIAAGVP VVPGSDGRLA DVAAAVAAAE AIGYPVMIKA AAGGGGRGIR VADTADDLRR
LVPQAQAEAQ AAFGDGGFYL ERVVRDARHI EVQIVGDGSR AVHCFERECS LQRRRQKVWE
EAPAACLDDA TRAELCRSAV ALAESVGYRG AGTLEYLYEP ASGAFFFIEM NTRIQVEHPV
TEMVTGVDLI AEMIRIAGGA PLSLRQEDIR LTGHAVEVRI NAEDPTNNFM PFPGVVGTLV
IPEGEGLRFD GMIYDGYAIP PFYDSLLGKL IVHGPDRGAA IDRLAAALRT LRVDGVKTTA
PLHVALAADP AVRAGDFHTQ FLEPWLAGRS LAAE
//
