ID F5YRG0_TREPZ Unreviewed; 443 AA.
AC F5YRG0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Biotin carboxylase (Acetyl-CoA carboxylase subunit A) (ACC) {ECO:0000313|EMBL:AEF85731.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:AEF85731.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:AEF85731.1};
GN OrderedLocusNames=TREPR_1270 {ECO:0000313|EMBL:AEF85731.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF85731.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF85731.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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DR EMBL; CP001843; AEF85731.1; -; Genomic_DNA.
DR RefSeq; WP_015708808.1; NC_015578.1.
DR AlphaFoldDB; F5YRG0; -.
DR STRING; 545694.TREPR_1270; -.
DR KEGG; tpi:TREPR_1270; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_12; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEF85731.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT DOMAIN 1..437
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 443 AA; 48688 MW; B6F32F5AE6AE0348 CRC64;
MIKRLLIANR GEIAVRIIRT CREMGIETTA VYSTADQDSL HVRMADRAVC IGPPPSSQSY
LNVNNLIMAA VNTGCEAIHP GVGFLSENAA FARTVRDRGL IFIGPDPETI ALLGDKVRAK
NTAEKFGLPV TPGSGPMKDP KEALALIHEK LGFPVIIKAA AGGGGKGMRI VRAPEELAEN
LSIAAQEAEA NFADGTVFIE RYLENPRHVE LQILADGNGT VAVLGERDCT VQKNHQKLIE
ESPSPAVTPA MRERMAEGAV PLFRELKYQG AGTIEFLVEG ENFYFMEVNA RVQVEHPVSE
FVTGIDIIRQ QILSCTEGRM EIKPDRVRTE GWAMECRINA LSPGKITRLE IPGGPGVRFD
SFLYTGCVVP PHYDSMIAKL IVHGANREQA LARMERALEE LFIEGIKNNI ARQRWIINNT
TFRSGKFGTS YYSEIEKEAE SAL
//
