ID Q18G87_HALWD Unreviewed; 614 AA.
AC Q18G87;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Propionyl-CoA carboxylase biotin carboxylase component {ECO:0000313|EMBL:CAJ53013.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:CAJ53013.1};
GN Name=pccA {ECO:0000313|EMBL:CAJ53013.1};
GN OrderedLocusNames=HQ_2906A {ECO:0000313|EMBL:CAJ53013.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ53013.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ53013.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AM180088; CAJ53013.1; -; Genomic_DNA.
DR RefSeq; WP_011572124.1; NC_008212.1.
DR AlphaFoldDB; Q18G87; -.
DR STRING; 362976.HQ_2906A; -.
DR GeneID; 4193680; -.
DR KEGG; hwa:HQ_2906A; -.
DR eggNOG; arCOG01591; Archaea.
DR HOGENOM; CLU_000395_3_1_2; -.
DR Proteomes; UP000001975; 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:CAJ53013.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001975}.
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 490..548
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; 66284 MW; EAE7543E37101463 CRC64;
MFNKVLVANR GEIAVRVMRA CDELGVQTVA VYSEADRNAG HVQYADEAYN IGPARAADSY
LNHDAVIAAG NQAGADAIHP GYGFLAENAT FAAAVESTDM TWIGPSSDAM AQLGEKTKAR
SLMQSADVPV VPGTTDPVES ASEVESIAAE YGYPVAIKAE GGGGGRGLQV VRETDDVESK
LETAQREGEA YFDNDSVYVE KYLDEPRHIE VQIIADHHGN VRHLGERDCS LQRRHQKVIE
EAPSPALSPD LRDEIGEAAR RGVQAAAYTN AGTVEFLVED GEFYFMEVNT RIQVEHTVTE
AITGIDIVKW QLRVAAGEPL SFEQSDVITD GHAIEYRINA EKPDADFTPT TGTLTTYDPP
GGIGVRVDDA VRQGDSIGGD YDSMIAKVIV SANNRAECLA RSERALAEFD IDGIETIIPF
HQLMLTDERF CNGEHTTKYL DHELDPERIK RAVEQRGGST SDELSSDDVG SNDTIERAFT
VEVNNKRFDV TLTEETTPEV PLPDLESDAF EAASSDSNSR STRSRPDEAL TDTENDASTV
AAGDGEEVSA DMQGTILSVE VTEDDTIEAG DVVCVLEAMK MENDITCERG GTVSQVCVSA
GDSVDTGDPI VILE
//
