ID G0LLW3_HALWC Unreviewed; 614 AA.
AC G0LLW3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Propionyl-CoA carboxylase biotin carboxylase component {ECO:0000313|EMBL:CCC41083.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:CCC41083.1};
GN Name=pccA {ECO:0000313|EMBL:CCC41083.1};
GN OrderedLocusNames=Hqrw_3306 {ECO:0000313|EMBL:CCC41083.1};
OS Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC41083.1, ECO:0000313|Proteomes:UP000007954};
RN [1] {ECO:0000313|EMBL:CCC41083.1, ECO:0000313|Proteomes:UP000007954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16854 / JCM 12705 / C23
RC {ECO:0000313|Proteomes:UP000007954};
RX PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA Rampp M., Oesterhelt D.;
RT "Haloquadratum walsbyi: limited diversity in a global pond.";
RL PLoS ONE 6:E20968-E20968(2011).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; FR746099; CCC41083.1; -; Genomic_DNA.
DR RefSeq; WP_014556532.1; NC_017459.1.
DR AlphaFoldDB; G0LLW3; -.
DR GeneID; 12448117; -.
DR KEGG; hwc:Hqrw_3306; -.
DR HOGENOM; CLU_000395_3_1_2; -.
DR OrthoDB; 31083at2157; -.
DR Proteomes; UP000007954; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
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; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCC41083.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 539..614
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 453..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 66315 MW; 60DAA90795254D5D CRC64;
MFNKVLVANR GEIAVRVMRA CDELGVQTVA VYSEADRNAG HVQYADEAYN IGPARAADSY
LNHDAVIAAG NQAGADAIHP GYGFLAENAT FAAAVESTDM TWIGPSSDAM AQLGEKTKAR
SLMQSADVPV VPGTTDPVKS ASEVESIAAE YGYPVAIKAE GGGGGRGLQV VRETDDVESQ
LETAQREGEA YFDNDSVYVE KYLDEPRHIE VQIIADHHGN VRHLGERDCS LQRRHQKVIE
EAPSPALSPD LRDEIGEAAR RGVQAAAYTN AGTVEFLVED GEFYFMEVNT RIQVEHTVTE
AITGIDIVKW QLRVAAGEPL SFEQSDVITD GHAIEYRINA ERPDADFTPT TGTLTTYDPP
GGIGVRVDDA VRQGDSIGGD YDSMIAKVIV SANNRAECLA RSERALAEFD IDGIETIIPF
HQFMLTDERF CNGEHTTKYL DHELDPERIK RAVEQRGGST SDELSSDDVG SNDTIERAFT
VEVNNKRFDV TLTEETAPEV PLPDLESDAF EAASSDSNSR STRSRPDEAL TDTENDASTV
AAGDGEEVSA DMQGTILSVE VTEDDTIEAG DVVCVLEAMK MENDITCERG GTVSQVCVSA
GDSVDTGDPI VILE
//
