ID T5D1Z8_HELPX Unreviewed; 280 AA.
AC T5D1Z8;
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=N407_05065 {ECO:0000313|EMBL:EQL70143.1};
OS Helicobacter pylori FD662.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191284 {ECO:0000313|EMBL:EQL70143.1, ECO:0000313|Proteomes:UP000015970};
RN [1] {ECO:0000313|EMBL:EQL70143.1, ECO:0000313|Proteomes:UP000015970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD662 {ECO:0000313|EMBL:EQL70143.1,
RC ECO:0000313|Proteomes:UP000015970};
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:EQL70143.1, ECO:0000313|Proteomes:UP000015970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD662 {ECO:0000313|EMBL:EQL70143.1,
RC ECO:0000313|Proteomes:UP000015970};
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:EQL70143.1}.
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; AKHT02000018; EQL70143.1; -; Genomic_DNA.
DR AlphaFoldDB; T5D1Z8; -.
DR PATRIC; fig|1191284.5.peg.1023; -.
DR Proteomes; UP000015970; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 1..280
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 1..154
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EQL70143.1"
SQ SEQUENCE 280 AA; 31940 MW; 8548C81576322DEB CRC64;
GRGMRVVEDK SKLKNLYLAA ETEALSAFGD GSVYLEKFIN KPKHIEVQIL ADKHGNVIHV
GERDCSVQRR QQKLIEETPA VVLEEGVRKR LLETAIKAAK YIGYVGAGTF EFLLDSNMKD
FYFMEMNTRL QVEHTISEMV SGLNLIEWMI KIAQGEELPK QESVSLKGHA IECRITAEDP
KKFYPSPGKI TEWIAPGGVN VRLDSHAHAH YVVPTHYDSM IGKLIVWGEN RERAIAKMKR
ALKEFKVEGI KTTIPFHLEM LENADFRQAK IHTKYLEENF
//
