ID T5CJB0_HELPX Unreviewed; 284 AA.
AC T5CJB0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Acetyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=N404_07675 {ECO:0000313|EMBL:EQL53259.1};
OS Helicobacter pylori FD506.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191281 {ECO:0000313|EMBL:EQL53259.1, ECO:0000313|Proteomes:UP000015964};
RN [1] {ECO:0000313|EMBL:EQL53259.1, ECO:0000313|Proteomes:UP000015964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD506 {ECO:0000313|EMBL:EQL53259.1,
RC ECO:0000313|Proteomes:UP000015964};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL53259.1, ECO:0000313|Proteomes:UP000015964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD506 {ECO:0000313|EMBL:EQL53259.1,
RC ECO:0000313|Proteomes:UP000015964};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQL53259.1}.
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DR EMBL; AKHO02000080; EQL53259.1; -; Genomic_DNA.
DR AlphaFoldDB; T5CJB0; -.
DR PATRIC; fig|1191281.5.peg.232; -.
DR Proteomes; UP000015964; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
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; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 1..284
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 2..158
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EQL53259.1"
SQ SEQUENCE 284 AA; 32265 MW; 5B7493ECA75B26E1 CRC64;
AGGGGRGMRV VEDKSKLKNL YLAAETEALS AFGDGSVYLE KFINKPKHIE VQILADKHGN
VIHVGERDCS VQRRQQKLIE ETPAVVLEES VRERLLETAI KAAKYISYVG AGTFEFLLDS
NMKDFYFMEM NTRLQVEHTI SEMVSGLNLI EWMIKIAQGE KLPKQESFSL KGHAIECRIT
AEDPKKFYPS PGKITEWIAP GGVNVRLDSH AHAHYVVPTH YDSMIGKLIV WGENRERAIA
KMKRALKEFK VEGIKTTIPF HLEMLENADF MQAKIHTKYL EENF
//
