ID Q4K800_PSEF5 Unreviewed; 457 AA.
AC Q4K800;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Putative acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:AAY93796.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:AAY93796.1};
GN OrderedLocusNames=PFL_4549 {ECO:0000313|EMBL:AAY93796.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY93796.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY93796.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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DR EMBL; CP000076; AAY93796.1; -; Genomic_DNA.
DR RefSeq; WP_011062805.1; NC_004129.6.
DR AlphaFoldDB; Q4K800; -.
DR STRING; 220664.PFL_4549; -.
DR KEGG; pfl:PFL_4549; -.
DR PATRIC; fig|220664.5.peg.4652; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_6; -.
DR Proteomes; UP000008540; Chromosome.
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; 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; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AAY93796.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 4..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 457 AA; 49094 MW; 02D15304230972E6 CRC64;
MTGSINKLLV ANRGEIAVRI IRAAKALGIP TVAACSEADA DSMAARMADE VQIIGPARAD
KSYLNVQALL GALQASGANA VHPGYGFLSE NADFAEAVVE AGAIFVGPSA ETIRRMGDKA
EARRTAQAAG VPVVPGSPGE LFDLDAALKA AEAVGFPLLI KASAGGGGRG IRLARDAAQL
TEEFPRAQRE AQTAFGNGAV YLERFIGRAR HIEVQVLGDG KHAVHLFERE CSLQRRRQKI
FEEAPSPVLS AEQREQLCSS AVRLTEALGY QGAGTLEYLY DDSTGEFFFI EMNTRIQVEH
PISELITGID LVQAMLRIAG GEPLGLRQSD IRLNGAALQM RLNAEDPARD FFPSPGKVEQ
LIWPQGAGVR VDSHLYPGYA VPPYYDSLLA KLIVHGRDRG EALARARIAV EHTTLTGMAS
TLSLHRELLA EPWLEQADFH TGTLETWLAE RRAGGVA
//
